Structure of PDB 1qia Chain A

Receptor sequence
>1qiaA (length=162) Species: 9606 (Homo sapiens) [Search protein sequence]
IPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEG
EADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTK
DTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQDD
INGIQSLYGPPP
3D structure
PDB1qia X-ray structure of human stromelysin catalytic domain complexed with nonpeptide inhibitors: implications for inhibitor selectivity
ChainA
Resolution2.0 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) H113 E114 H117 H123
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 ZN A H201 H205 H211 H113 H117 H123
BS02 ZN A H151 D153 H166 H179 H63 D65 H78 H91
BS03 CA A D158 G159 G161 V163 D181 E184 D70 G71 G73 V75 D93 E96
BS04 CA A D141 G173 N175 D177 D53 G85 N87 D89
BS05 CA A D107 D182 E184 D19 D94 E96
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:1qia, PDBe:1qia, PDBj:1qia
PDBsum1qia
PubMed10422833
UniProtP08254|MMP3_HUMAN Stromelysin-1 (Gene Name=MMP3)

[Back to BioLiP]