Structure of PDB 2srt Chain A

Receptor sequence
>2srtA (length=173) Species: 9606 (Homo sapiens) [Search protein sequence]
FRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTF
SRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDD
DEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRF
RLSQDDINGIQSLYGPPPDSPET
3D structure
PDB2srt The NMR structure of the inhibited catalytic domain of human stromelysin-1.
ChainA
ResolutionN/A
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H201 E202 H205 H211
Catalytic site (residue number reindexed from 1) H119 E120 H123 H129
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 H119 H123 H129
BS02 ZN A H151 Y155 H166 H179 H69 Y73 H84 H97
BS03 8MI A N162 V163 L164 A165 L197 H201 H211 L218 L222 Y223 N80 V81 L82 A83 L115 H119 H129 L136 L140 Y141
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

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Cellular Component
External links
PDB RCSB:2srt, PDBe:2srt, PDBj:2srt
PDBsum2srt
PubMed7656014
UniProtP08254|MMP3_HUMAN Stromelysin-1 (Gene Name=MMP3)

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