Structure of PDB 1eak Chain B Binding Site BS05

Receptor Information
>1eak Chain B (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
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain1eak Chain B Residue 999 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
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)		D168 G200 G202
Binding residue
(residue number reindexed from 1)		D137 G169 G171
Annotation score4
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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