Structure of PDB 1sln Chain A

Receptor sequence

>1slnA (length=168) Species: 9606 (Homo sapiens) [Search protein sequence]

FRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTF
SRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDD
DEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRF
RLSQDDINGIQSLYGPPP

3D structure

PDB

1sln Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme.

Chain

Resolution

2.27 Å

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)
BS01	ZN	A	H201 H205 H211	H119 H123 H129
BS02	ZN	A	H151 D153 H166 H179	H69 D71 H84 H97
BS03	CA	A	D158 G159 G161 V163 D181 E184	D76 G77 G79 V81 D99 E102
BS04	CA	A	D141 G173 N175 D177	D59 G91 N93 D95
BS05	CA	A	D107 D182 E184	D25 D100 E102
BS06	8MI	A	N162 L164 A165 L197 V198 H201 E202 H205 H211 L222 Y223	N80 L82 A83 L115 V116 H119 E120 H123 H129 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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Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:1sln, PDBe:1sln, PDBj:1sln
PDBsum	1sln
PubMed	8535233
UniProt	P08254\|MMP3_HUMAN Stromelysin-1 (Gene Name=MMP3)

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