Structure of PDB 1mmq Chain A

Receptor sequence
>1mmqA (length=166) Species: 9606 (Homo sapiens) [Search protein sequence]
YSLFPNSPKWTSKVVTYRIVSYTRDLPHITVDRLVSKALNMWGKEIPLHF
RKVVWGTADIMIGFARGAHGDSYPFDGPGNTLAHAFAPGTGLGGDAHFDE
DERWTDGSSLGINFLYAATHELGHSLGMGHSSDPNAVMYPTYGNGDPQNF
KLSQDDIKGIQKLYGK
3D structure
PDB1mmq Matrilysin-inhibitor complexes: common themes among metalloproteases.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H218 E219 H222 H228
Catalytic site (residue number reindexed from 1) H120 E121 H124 H130
Enzyme Commision number 3.4.24.23: matrilysin.
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 H218 H222 H228 H120 H124 H130
BS02 ZN A H168 D170 H183 H196 H69 D71 H84 H97
BS03 CA A D175 G176 G178 T180 D198 E201 D76 G77 G79 T81 D99 E102
BS04 CA A D158 G190 G192 D194 D59 G91 G93 D95
BS05 RRS A N179 L181 A182 H218 E219 H222 H228 P238 T239 Y240 N80 L82 A83 H120 E121 H124 H130 P140 T141 Y142 MOAD: Ki=0.03uM
PDBbind-CN: -logKd/Ki=7.52,Ki=0.03uM
BindingDB: Ki=3nM
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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Cellular Component
External links
PDB RCSB:1mmq, PDBe:1mmq, PDBj:1mmq
PDBsum1mmq
PubMed7756291
UniProtP09237|MMP7_HUMAN Matrilysin (Gene Name=MMP7)

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