Structure of PDB 1rm8 Chain A

Receptor sequence
>1rm8A (length=169) Species: 9606 (Homo sapiens) [Search protein sequence]
GQKWQHKHITYSIKNVTPKVGDPETRKAIRRAFDVWQNVTPLTFEEVPYS
ELENGKRDVDITIIFASGFHGDSSPFDGEGGFLAHAYFPGPGIGGDTHFD
SDEPWTLGNPNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMET
DNFKLPNDDLQGIQKIYGP
3D structure
PDB1rm8 Crystal structure of the catalytic domain of MMP-16/MT3-MMP: characterization of MT-MMP specific features.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H246 E247 H250 H256
Catalytic site (residue number reindexed from 1) H123 E124 H127 H133
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 A H246 H250 H256 H123 H127 H133
BS02 ZN A H193 D195 H208 H221 H70 D72 H85 H98
BS03 CA A D200 G201 G203 F205 D223 E226 D77 G78 G80 F82 D100 E103
BS04 CA A D183 G215 I216 G217 D219 D60 G92 I93 G94 D96
BS05 BAT A G204 F205 L206 A207 V243 H246 E247 H250 H256 P266 F267 Y268 G81 F82 L83 A84 V120 H123 E124 H127 H133 P143 F144 Y145 PDBbind-CN: -logKd/Ki=9.00,Ki=1nM
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:1rm8, PDBe:1rm8, PDBj:1rm8
PDBsum1rm8
PubMed14741217
UniProtP51512|MMP16_HUMAN Matrix metalloproteinase-16 (Gene Name=MMP16)

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