BioLiP

Structure of PDB 1bm6 Chain A

Receptor sequence

>1bm6A (length=173) Species: 9606 (Homo sapiens) [Search protein sequence]

FRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTF
SRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDD
DEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRF
RLSQDDINGIQSLYGPPPDSPET

3D structure

PDB

1bm6 Solution structure of the catalytic domain of human stromelysin-1 complexed to a potent, nonpeptidic inhibitor.

Chain

Resolution

N/A

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)	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 F157 H166 H179	H69 F75 H84 H97
BS03	CA	A	D158 G159 G161 V163 D181 E184	D76 G77 G79 V81 D99 E102
BS04	CA	A	D141 G173 N175 G176 D177	D59 G91 N93 G94 D95
BS05	HAV	A	V163 A165 H201 H205	V81 A83 H119 H123	PDBbind-CN: -logKd/Ki=7.89,Ki=13nM
BS06	MSB	A	N162 L164 V198 H201 L218 M219 P221 L222	N80 L82 V116 H119 L136 M137 P139 L140	PDBbind-CN: -logKd/Ki=7.89,Ki=13nM

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

PDB	RCSB:1bm6, PDBe:1bm6, PDBj:1bm6
PDBsum	1bm6
PubMed	9760240
UniProt	P08254\|MMP3_HUMAN Stromelysin-1 (Gene Name=MMP3)