Structure of PDB 1c3i Chain B

Receptor sequence

>1c3iB (length=173) Species: 9606 (Homo sapiens) [Search protein sequence]

FRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTF
SRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDD
DEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRF
RLSQDDINGIQSLYGPPPDSPET

3D structure

PDB

1c3i Expression, characterization and structure determination of an active site mutant (Glu202-Gln) of mini-stromelysin-1.

Chain

Resolution

1.83 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)	Binding affinity
BS01	ZN	B	H201 H205 H211	H119 H123 H129
BS02	ZN	B	H151 D153 H166 H179	H69 D71 H84 H97
BS03	CA	B	D107 D182 E184	D25 D100 E102
BS04	CA	B	D141 G173 N175 D177	D59 G91 N93 D95
BS05	CA	B	D158 G159 G161 V163 D181 E184	D76 G77 G79 V81 D99 E102
BS06	TR1	B	N162 V163 L164 A165 V198 H201 E202 H205 H211 L218 Y220 P221 L222 Y223	N80 V81 L82 A83 V116 H119 E120 H123 H129 L136 Y138 P139 L140 Y141	PDBbind-CN: -logKd/Ki=5.80,IC50=1.6uM

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:1c3i, PDBe:1c3i, PDBj:1c3i
PDBsum	1c3i
PubMed	10877850
UniProt	P08254\|MMP3_HUMAN Stromelysin-1 (Gene Name=MMP3)

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