Structure of PDB 1buv Chain M

Receptor sequence
>1buvM (length=174) Species: 9606 (Homo sapiens) [Search protein sequence]
IQGLKWQHNEITFCIQNYTPKVGEYATYEAIRKAFRVWESATPLRFREVP
YAYIREGHEKQADIMIFFAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDT
HFDSAEPWTVRNEDLNGNDIFLVAVHELGHALGLEHSSDPSAIMAPFYQW
MDTENFVLPDDDRRGIQQLYGGES
3D structure
PDB1buv Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor.
ChainM
Resolution2.75 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H239 H243 H249
Catalytic site (residue number reindexed from 1) H126 H130 H136
Enzyme Commision number 3.4.24.80: membrane-type matrix metalloproteinase-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 CA M D176 N208 G210 D63 N95 G97
BS02 ZN M H239 H243 H249 H126 H130 H136
BS03 ZN M H186 D188 H201 H214 H73 D75 H88 H101
BS04 CA M D193 G194 G196 F198 D216 E219 D80 G81 G83 F85 D103 E106
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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Cellular Component
External links
PDB RCSB:1buv, PDBe:1buv, PDBj:1buv
PDBsum1buv
PubMed9724659
UniProtP50281|MMP14_HUMAN Matrix metalloproteinase-14 (Gene Name=MMP14)

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