Structure of PDB 1hv5 Chain F

Receptor sequence
>1hv5F (length=162) Species: 10090 (Mus musculus) [Search protein sequence]
MFVLSGGRWEKTDLTYRILRFPWQLVREQVRQTVAEALQVWSEVTPLTFT
EVHEGRADIMIDFARYWHGDNLPFDGPGGILAHAFFPKTHREGDVHFDYD
ETWTIGDNQGTDLLQVAAHEFGHVLGLQHTTAAKALMSPFYTFRYPLSLS
PDDRRGIQHLYG
3D structure
PDB1hv5 Crystal structure of the stromelysin-3 (MMP-11) catalytic domain complexed with a phosphinic inhibitor mimicking the transition-state.
ChainF
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H219 E220 H223 H229
Catalytic site (residue number reindexed from 1) H119 E120 H123 H129
Enzyme Commision number 3.4.24.-
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 F H168 D170 H183 H196 H68 D70 H83 H96
BS02 ZN F H219 H223 H229 H119 H123 H129
BS03 CA F D175 G176 G178 I180 D198 E201 D75 G76 G78 I80 D98 E101
BS04 RXP F L172 G179 I180 L181 A182 A184 H219 E220 H229 F240 Y241 L72 G79 I80 L81 A82 A84 H119 E120 H129 F140 Y141 BindingDB: Ki=5nM
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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Biological Process
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Cellular Component
External links
PDB RCSB:1hv5, PDBe:1hv5, PDBj:1hv5
PDBsum1hv5
PubMed11254383
UniProtQ02853|MMP11_MOUSE Stromelysin-3 (Gene Name=Mmp11)

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