Structure of PDB 1eak Chain B Binding Site BS01
Receptor Information
>1eak Chain B (length=419) Species:
9606
(Homo sapiens) [
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SPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFF
GLPQTGDLDQNTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGY
TPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDG
YPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGE
YCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFT
MGGNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGF
CPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANY
DDDRKWGFCPDQGYSLFLVAAHQFGHAMGLEHSQDPGALMAPIYTYTKNF
RLSQDDIKGIQELYGASPD
Ligand information
>1eak Chain R (length=8) Species:
32630
(synthetic construct) [
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GPAGPPGA
Receptor-Ligand Complex Structure
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PDB
1eak
Crystal Structure of Human Mmp-2 Reveals a New P
Resolution
2.66 Å
Binding residue
(original residue number in PDB)
R296 G299 T300 S301
Binding residue
(residue number reindexed from 1)
R265 G268 T269 S270
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
PDBsum
1eak
PubMed
UniProt
P08253
|MMP2_HUMAN 72 kDa type IV collagenase (Gene Name=MMP2)
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