1AV1ACD

Crystal structure of human apolipoprotein a-i
Link type Probability Chain A piercings Chain C piercings Chain D piercings
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6SUP3_3.2 6SUP3_3.2 50% +54C +58D -83D +243D -219A -222D -243A -57C
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6SUP3_3.2 6SUP3_3.2 50% +54C +58D -83D +243D -219A -222D -243A -57C
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6SUP3_3.2 6SUP3_3.2 50% +54C +58D -83D +243D -219A -222D -243A -57C
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6SUP3_3.2 6SUP3_3.2 50% +54C +58D -83D +243D -219A -222D -243A -57C
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6SUP3_3.2 6SUP3_3.2 50% +54C +58D -83D +243D -219A -222D -243A -57C
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6SUP3_3.2 6SUP3_3.2 50% +54C +58D -83D +243D -219A -222D -243A -57C
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6SUP3_3.2 6SUP3_3.2 50% +54C +58D -83D +243D -219A -222D -243A -57C
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6SUP3_3.2 6SUP3_3.2 50% +54C +58D -83D +243D -219A -222D -243A -57C
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6SUP3_3.2 6SUP3_3.2 50% +54C +58D -83D +243D -219A -222D -243A -57C
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6SUP3_3.2 6SUP3_3.2 50% +54C +58D -83D +243D -219A -222D -243A -57C
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6SUP3_3.2 6SUP3_3.2 50% +54C +58D -83D +243D -219A -222D -243A -57C
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6SUP3_3.2 6SUP3_3.2 50% +54C +58D -83D +243D -219A -222D -243A -57C
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6SUP3_3.2 6SUP3_3.2 50% +54C +58D -83D +243D -219A -222D -243A -57C
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6SUP3_3.2 6SUP3_3.2 50% +54C +58D -83D +243D -219A -222D -243A -57C
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6SUP3_3.2 6SUP3_3.2 50% +54C +58D -83D +243D -219A -222D -243A -57C
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6SUP3_3.2 6SUP3_3.2 50% +54C +58D -83D +243D -219A -222D -243A -57C
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6SUP3_3.2 6SUP3_3.2 50% +54C +58D -83D +243D -219A -222D -243A -57C
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6SUP3_3.2 6SUP3_3.2 50% +54C +58D -83D +243D -219A -222D -243A -57C
Interpreting sequences
Chain A Sequence
MLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ
Chain A Sequence
MLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ
Chain A Sequence
MLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ
sequence length 201,201,201
structure length 201,201,201
publication title Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation.
pubmed doi rcsb
molecule tags Lipid transport
molecule keywords APOLIPOPROTEIN A-I
source organism Homo sapiens
pdb deposition date1997-09-23
LinkProt deposition date2016-08-17

pfam database annotations

chain Pfam Accession CodePfam Family IdentifierPfam Description
ACD PF01442 ApolipoproteinApolipoprotein A1/A4/E domain
ACD PF01442 ApolipoproteinApolipoprotein A1/A4/E domain
ACD PF01442 ApolipoproteinApolipoprotein A1/A4/E domain
Image from the rcsb pdb (www.rcsb.org)
cath code
ClassArchitectureTopologyHomologyDomain
1.20.5.1230 Mainly Alpha Up-down Bundle Single alpha-helices involved in coiled-coils or other helix-helix interfaces Apolipoprotein A-I 1av1C00
1AV1CD 1AV1ABCD 1AV1ACD 1AV1AC 1AV1BCD 1AV1ABC 1AV1BC
chains in the LinkProt database with same CATH superfamily
1OW6BD 1MV8BCD 1OW6ABF 1MUUABCD 1MV8CD 1OW6BF 1MUUAC 1OW6BCF 3EFFKMN 1MUUAB 1MUUBD 1MV8BD 3EFFAN 1MUUBCD 1OW6AB 3EFFLMN 1OW6ABC 1OW6ABCF 1AV1CD 1OW6BDF 1OW6AD 1MV8AB 1AV1BCD 1AV1ABC 3EFFBN 3EFFCL 3EFFDK 1MV8AC 3EFFKN 1AQ5BC 3EFFAM 1AQ5AB 1AV1ABCD 2P1JAB 3EFFDL 1AV1AC 3EFFCK 1MFZCD 1OW6BC 1MUUCD 1MUUABD 1QEXAB 1MV8ABC 1OW6BCD 1AQ5AC 1MV8ABD 1MFZAB 1MUUACD 1OW6ABDF 1AV1BC 1MV8ACD 1MUUABC 3EFFMN 1OW6CF 3EFFAK 1OW6ABD 1AQ5ABC 3EFFBM 3EFFKL 1AV1ACD 1OW6ABCD 1OW6BCDF 1MV8ABCD
chains in the LinkProt database with same CATH topology
1AV1CD 1AV1ABCD 1AV1ACD 1AV1AC 1AV1BCD 1AV1ABC 1AV1BC
chains in the LinkProt database with same CATH homology


 
#chains in the LinkProt database with same CATH superfamily
 1AV1 CD;  1AV1 ABCD;  1AV1 ACD;  1AV1 AC;  1AV1 BCD;  1AV1 ABC;  1AV1 BC; 
#chains in the LinkProt database with same CATH topology
 1OW6 BD;  1MV8 BCD;  1OW6 ABF;  1MUU ABCD;  1MV8 CD;  1OW6 BF;  1MUU AC;  1OW6 BCF;  3EFF KMN;  1MUU AB;  1MUU BD;  1MV8 BD;  3EFF AN;  1MUU BCD;  1OW6 AB;  3EFF LMN;  1OW6 ABC;  1OW6 ABCF;  1AV1 CD;  1OW6 BDF;  1OW6 AD;  1MV8 AB;  1AV1 BCD;  1AV1 ABC;  3EFF BN;  3EFF CL;  3EFF DK;  1MV8 AC;  3EFF KN;  1AQ5 BC;  3EFF AM;  1AQ5 AB;  1AV1 ABCD;  2P1J AB;  3EFF DL;  1AV1 AC;  3EFF CK;  1MFZ CD;  1OW6 BC;  1MUU CD;  1MUU ABD;  1QEX AB;  1MV8 ABC;  1OW6 BCD;  1AQ5 AC;  1MV8 ABD;  1MFZ AB;  1MUU ACD;  1OW6 ABDF;  1AV1 BC;  1MV8 ACD;  1MUU ABC;  3EFF MN;  1OW6 CF;  3EFF AK;  1OW6 ABD;  1AQ5 ABC;  3EFF BM;  3EFF KL;  1AV1 ACD;  1OW6 ABCD;  1OW6 BCDF;  1MV8 ABCD; 
#chains in the LinkProt database with same CATH homology
 1AV1 CD;  1AV1 ABCD;  1AV1 ACD;  1AV1 AC;  1AV1 BCD;  1AV1 ABC;  1AV1 BC; 

1AV1B 1AV1C 1AV1D 6CLZB 6CLZC 6CM1B 6CM1C 6CCHA 6CCHC 6CCXA 6CCXC 6CC9A 6CC9C 2MSCA 2MSCC 2MSDA 2MSDC 2MSEA 2MSEC 4V6MA0 4V6MA1 1AV1A 1AV1B 1AV1D 6CLZB 6CLZC 6CM1B 6CM1C 6CCHA 6CCHC 6CCXA 6CCXC 6CC9A 6CC9C 2MSCA 2MSCC 2MSDA 2MSDC 2MSEA 2MSEC 4V6MA0 4V6MA1 1AV1A 1AV1B 1AV1C 6CLZB 6CLZC 6CM1B 6CM1C 6CCHA 6CCHC 6CCXA 6CCXC 6CC9A 6CC9C 2MSCA 2MSCC 2MSDA 2MSDC 2MSEA 2MSEC 4V6MA0 4V6MA1
similar chains in the pdb database (40% sequence similarity)

 
            
               
               
           
#similar chains in the pdb database (40% sequence similarity)
 1AV1_B;  1AV1_C;  1AV1_D;  6CLZ_B;  6CLZ_C;  6CM1_B;  6CM1_C;  6CCH_A;  6CCH_C;  6CCX_A;  6CCX_C;  6CC9_A;  6CC9_C;  2MSC_A;  2MSC_C;  2MSD_A;  2MSD_C;  2MSE_A;  2MSE_C;  4V6M_A0;  4V6M_A1;  1AV1_A;  1AV1_B;  1AV1_D;  6CLZ_B;  6CLZ_C;  6CM1_B;  6CM1_C;  6CCH_A;  6CCH_C;  6CCX_A;  6CCX_C;  6CC9_A;  6CC9_C;  2MSC_A;  2MSC_C;  2MSD_A;  2MSD_C;  2MSE_A;  2MSE_C;  4V6M_A0;  4V6M_A1;  1AV1_A;  1AV1_B;  1AV1_C;  6CLZ_B;  6CLZ_C;  6CM1_B;  6CM1_C;  6CCH_A;  6CCH_C;  6CCX_A;  6CCX_C;  6CC9_A;  6CC9_C;  2MSC_A;  2MSC_C;  2MSD_A;  2MSD_C;  2MSE_A;  2MSE_C;  4V6M_A0;  4V6M_A1; 
           

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