Structure of PDB 1eak Chain D Binding Site BS01

Receptor Information
>1eak Chain D (length=419) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFF
GLPQTGDLDQNTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGY
TPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDG
YPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGE
YCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFT
MGGNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGF
CPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANY
DDDRKWGFCPDQGYSLFLVAAHQFGHAMGLEHSQDPGALMAPIYTYTKNF
RLSQDDIKGIQELYGASPD
Ligand information
Receptor-Ligand Complex Structure
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PDB1eak Crystal Structure of Human Mmp-2 Reveals a New P
Resolution2.66 Å
Binding residue
(original residue number in PDB)		P133 D209 H276 E277 A278 F293 S304
Binding residue
(residue number reindexed from 1)		P102 D178 H245 E246 A247 F262 S273
Enzymatic activity
Catalytic site (original residue number in PDB) H403 Q404 H407 H413
Catalytic site (residue number reindexed from 1) H372 Q373 H376 H382
Enzyme Commision number 3.4.24.24: gelatinase A.
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:1eak, PDBe:1eak, PDBj:1eak
PDBsum1eak
PubMed
UniProtP08253|MMP2_HUMAN 72 kDa type IV collagenase (Gene Name=MMP2)

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