Structure of PDB 4ayk Chain A

Receptor sequence
>4aykA (length=169) Species: 9606 (Homo sapiens) [Search protein sequence]
VLTEGNPRWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFT
KVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDED
ERWTNNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSYTFSGDVQLAQ
DDIDGIQAIYGRSQNPVQP
3D structure
PDB4ayk NMR solution structure of the catalytic fragment of human fibroblast collagenase complexed with a sulfonamide derivative of a hydroxamic acid compound.
ChainA
ResolutionN/A
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) H118 E119 H122 H128
Catalytic site (residue number reindexed from 1) H118 E119 H122 H128
Enzyme Commision number 3.4.24.7: interstitial collagenase.
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 ZN A H118 H122 H128 H118 H122 H128
BS02 ZN A H68 H83 H96 H68 H83 H96
BS03 CA A G76 P77 G78 D98 E101 G76 P77 G78 D98 E101
BS04 CGS A N80 L81 A82 R114 H118 H122 H128 P138 S139 N80 L81 A82 R114 H118 H122 H128 P138 S139 BindingDB: Ki=33nM,IC50=15nM
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0031012 extracellular matrix

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4ayk, PDBe:4ayk, PDBj:4ayk
PDBsum4ayk
PubMed10353819
UniProtP03956|MMP1_HUMAN Interstitial collagenase (Gene Name=MMP1)

[Back to BioLiP]