Structure of PDB 3ma2 Chain A

Receptor sequence
>3ma2A (length=168) Species: 9606 (Homo sapiens) [Search protein sequence]
LKWQHNEITFCIQNYTPKVGEYATYEAIRKAFRVWESATPLRFREVPYAY
IREGHEKQADIMIFFAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDTHFD
SAEPWTVRNEDLNGNDIFLVAVHELGHALGLEHSSDPSAIMAPFYQWMDT
ENFVLPDDDRRGIQQLYG
3D structure
PDB3ma2 The Intrinsic Protein Flexibility of Endogenous Protease Inhibitor TIMP-1 Controls Its Binding Interface and Affects Its Function.
ChainA
Resolution2.05 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 E240 H243 H249
Catalytic site (residue number reindexed from 1) H123 E124 H127 H133
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 A D176 N208 G210 D212 D60 N92 G94 D96
BS02 ZN A H239 H243 H249 H123 H127 H133
BS03 ZN A H186 D188 H201 H214 H70 D72 H85 H98
BS04 CA A D193 G194 G196 F198 D216 E219 D77 G78 G80 F82 D100 E103
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:3ma2, PDBe:3ma2, PDBj:3ma2
PDBsum3ma2
PubMed20545310
UniProtP50281|MMP14_HUMAN Matrix metalloproteinase-14 (Gene Name=MMP14)

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