Structure of PDB 5mhl Chain B

Receptor sequence
>5mhlB (length=697) Species: 9606 (Homo sapiens) [Search protein sequence]
PPNNSNAAEDDLPTVELQGVVPRGVNLQEFLNVTSVHLFKERWDTNKVDH
HTDKYENNKLIVRRGQSFYVQIDFSRPYDPRRDLFRVEYVIGRYPQENKG
TYIPVPIVSELQSGKWGAKIVMREDRSVRLSIQSSPKCIVGKFRMYVAVW
TPYGVLRTSRNPETDTYILFNPWCEDDAVYLDNEKEREEYVLNDIGVIFY
GEVNDIKTRSWSYGQFEDGILDTCLYVMDRAQMDLSGRGNPIKVSRVGSA
MVNAKDDEGVLVGSWDNIYAYGVPPSAWTGSVDILLEYRSSENPVRYGQC
WVFAGVFNTFLRCLGIPARIVTNYFSAHDNDANLQMDIFLEEDGNVNSKL
TKDSVWNYHCWNEAWMTRPDLPVGFGGWQAVDSTPQENSDGMYRCGPASV
QAIKHGHVCFQFDAPFVFAEVNSDLIYITAHVVENVDATHIGKLIVTKQI
GGDGMMDITDTYKFQEGQEEERLALETALMYGRSNVDMDFEVENAVLGKD
FKLSITFRNNSHNRYTITAYLSANITFYTGVPKAEFKKETFDVTLEPLSF
KKEAVLIQAGEYMGQLLEQASLHFFVTARINETRDVLAKQKSTVLTIPEI
IIKVRGTQVVSDMTVIVEFTNPLKETLRNVWVHLDGPGVTRPMKKMFREI
RPNSTVQWEEVCRPWVSGHRKLIASMSSDSLRHVYGELDVQIQRRPS
3D structure
PDB5mhl Structure of active coagulation factor XIII triggered by calcium binding: basis for the design of next-generation anticoagulants.
ChainB
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) W279 C314 H373 D396 Y560
Catalytic site (residue number reindexed from 1) W265 C300 H359 D382 Y528
Enzyme Commision number 2.3.2.13: protein-glutamine gamma-glutamyltransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 peptide B Y214 W279 C314 V369 W370 N371 Y372 H373 Y200 W265 C300 V355 W356 N357 Y358 H359
BS02 CA B D343 D345 N347 Q349 D351 D367 D329 D331 N333 Q335 D337 D353
BS03 CA B N436 A457 E485 E490 N422 A438 E466 E471
BS04 CA B A264 N267 K269 D271 A250 N253 K255 D257
Gene Ontology
Molecular Function
GO:0003810 protein-glutamine gamma-glutamyltransferase activity
GO:0005515 protein binding
GO:0016746 acyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0007596 blood coagulation
GO:0018149 peptide cross-linking
GO:0072378 blood coagulation, fibrin clot formation
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005737 cytoplasm
GO:0031093 platelet alpha granule lumen
GO:0062023 collagen-containing extracellular matrix
GO:0072562 blood microparticle
GO:1990234 transferase complex

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5mhl, PDBe:5mhl, PDBj:5mhl
PDBsum5mhl
PubMed
UniProtP00488|F13A_HUMAN Coagulation factor XIII A chain (Gene Name=F13A1)

[Back to BioLiP]