1K50ABCD

A v49a mutation induces 3d domain swapping in the b1 domain of protein l from peptostreptococcus magnus
Link type Probability Chain A piercings Chain B piercings Chain C piercings Chain D piercings
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Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
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Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
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Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
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Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
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Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
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Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
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Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
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Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
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Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
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Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
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Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
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Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
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Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
view details
Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
view details
Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
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Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
view details
Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
view details
Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
view details
Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
view details
Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
view details
Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
view details
Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
view details
Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
view details
Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
view details
Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
view details
Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
view details
Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
view details
Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
view details
Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
view details
Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
view details
Hopf.2 U 2 Rings Hopf.2 U 2 Rings 20% +21B -47B -64C -65D
Interpreting sequences
Chain A Sequence
EEVTIKANLIFANGSTQTAEFKGTFEKATSEAYAYADTLKKDNGEWTADVADKGYTLNIKFAG
Chain A Sequence
EEVTIKANLIFANGSTQTAEFKGTFEKATSEAYAYADTLKKDNGEWTADVADKGYTLNIKFAG
Chain A Sequence
EEVTIKANLIFANGSTQTAEFKGTFEKATSEAYAYADTLKKDNGEWTADVADKGYTLNIKFAG
Chain A Sequence
EEVTIKANLIFANGSTQTAEFKGTFEKATSEAYAYADTLKKDNGEWTADVADKGYTLNIKFAG
sequence length 63,63,63,63
structure length 63,63,63,63
publication title Single-site mutations induce 3D domain swapping in the B1 domain of protein L from Peptostreptococcus magnus.
pubmed doi rcsb
molecule tags Protein binding
molecule keywords Protein L
source organism Finegoldia magna
pdb deposition date2001-10-09
LinkProt deposition date2016-10-21

pfam database annotations

chain Pfam Accession CodePfam Family IdentifierPfam Description
ABCD PF02246 B1Protein L b1 domain
ABCD PF02246 B1Protein L b1 domain
ABCD PF02246 B1Protein L b1 domain
ABCD PF02246 B1Protein L b1 domain
Image from the rcsb pdb (www.rcsb.org)
cath code
ClassArchitectureTopologyHomologyDomain
3.10.20.10 Alpha Beta Roll Ubiquitin-like (UB roll) Ubiquitin-like (UB roll) 1k50A00
3.10.20.10 Alpha Beta Roll Ubiquitin-like (UB roll) Ubiquitin-like (UB roll) 1k50B00
3.10.20.10 Alpha Beta Roll Ubiquitin-like (UB roll) Ubiquitin-like (UB roll) 1k50C00
3.10.20.10 Alpha Beta Roll Ubiquitin-like (UB roll) Ubiquitin-like (UB roll) 1k50D00
1K50CD 1K50AC 1K50ABC 1K50BD 1K50BCD 1K50ABCD 1Q10AB 1K50BC 1K50ACD 1K50AB 1K50ABD 1K50AD
chains in the LinkProt database with same CATH superfamily
1K50AC 1K50BD 1Q10AB 2G45AB 1K50ACD 1K50BC 1P3QQRV 1K50AD 1K50ABCD 1K50AB 1K50ABD 2G45DE 2G45BDE 1K50CD 2G45ABD 2G45ADE 2G45AE 1AARAB 1P3QRV 2HJ1AB 1K50ABC 2G45ABE 1K50BCD 1P3QQV 2G45ABDE 2G45BD
chains in the LinkProt database with same CATH topology
1K50CD 1K50AC 1K50ABC 1K50BD 1K50BCD 1K50ABCD 1Q10AB 1K50BC 1K50ACD 1K50AB 1K50ABD 1K50AD
chains in the LinkProt database with same CATH homology


 
#chains in the LinkProt database with same CATH superfamily
 1K50 CD;  1K50 AC;  1K50 ABC;  1K50 BD;  1K50 BCD;  1K50 ABCD;  1Q10 AB;  1K50 BC;  1K50 ACD;  1K50 AB;  1K50 ABD;  1K50 AD; 
#chains in the LinkProt database with same CATH topology
 1K50 AC;  1K50 BD;  1Q10 AB;  2G45 AB;  1K50 ACD;  1K50 BC;  1P3Q QRV;  1K50 AD;  1K50 ABCD;  1K50 AB;  1K50 ABD;  2G45 DE;  2G45 BDE;  1K50 CD;  2G45 ABD;  2G45 ADE;  2G45 AE;  1AAR AB;  1P3Q RV;  2HJ1 AB;  1K50 ABC;  2G45 ABE;  1K50 BCD;  1P3Q QV;  2G45 ABDE;  2G45 BD; 
#chains in the LinkProt database with same CATH homology
 1K50 CD;  1K50 AC;  1K50 ABC;  1K50 BD;  1K50 BCD;  1K50 ABCD;  1Q10 AB;  1K50 BC;  1K50 ACD;  1K50 AB;  1K50 ABD;  1K50 AD; 
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#similar chains in the LinkProt database (?% sequence similarity)
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#similar chains, but unlinked
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#similar chains in the pdb database (?% sequence similarity)
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LinkProt | Interdisciplinary Laboratory of Biological Systems Modelling