Structure of PDB 6n9d Chain A

Receptor sequence
>6n9dA (length=161) Species: 9606 (Homo sapiens) [Search protein sequence]
PGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLY
EGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQW
TKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQ
DDINGIQSLYG
3D structure
PDB6n9d Directed evolution of the metalloproteinase inhibitor TIMP-1 reveals that its N- and C-terminal domains cooperate in matrix metalloproteinase recognition.
ChainA
Resolution2.67 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) H201 E202 H205 H211
Catalytic site (residue number reindexed from 1) H115 E116 H119 H125
Enzyme Commision number 3.4.24.17: stromelysin 1.
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 CA A D158 G159 G161 V163 D181 E184 D72 G73 G75 V77 D95 E98
BS02 CA A D107 D182 D21 D96
BS03 ZN A H151 D153 H166 H179 H65 D67 H80 H93
BS04 ZN A H201 H205 H211 H115 H119 H125
BS05 CA A D141 G173 N175 D177 D55 G87 N89 D91
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:6n9d, PDBe:6n9d, PDBj:6n9d
PDBsum6n9d
PubMed31040180
UniProtP08254|MMP3_HUMAN Stromelysin-1 (Gene Name=MMP3)

[Back to BioLiP]