Structure of PDB 1slm Chain A

Receptor sequence
>1slmA (length=226) Species: 9606 (Homo sapiens) [Search protein sequence]
LVQKYLENYYDLKKDSGPVVKKIREMQKFLGLEVTGKLDSDTLEVMRKPR
CGVPDVGHFRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVW
EEVTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGI
NGDAHFDDDEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYH
SLTDLTRFRLSQDDINGIQSLYGPPP
3D structure
PDB1slm Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme.
ChainA
Resolution1.9 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) H177 E178 H181 H187
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 C75 H201 H205 H211 C51 H177 H181 H187
BS02 ZN A H151 D153 H166 H179 H127 D129 H142 H155
BS03 CA A D158 G159 G161 V163 D181 E184 D134 G135 G137 V139 D157 E160
BS04 CA A D141 G173 N175 D177 D117 G149 N151 D153
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:1slm, PDBe:1slm, PDBj:1slm
PDBsum1slm
PubMed8535233
UniProtP08254|MMP3_HUMAN Stromelysin-1 (Gene Name=MMP3)

[Back to BioLiP]