Structure of PDB 1eak Chain C

Receptor sequence
>1eakC (length=418) Species: 9606 (Homo sapiens) [Search protein sequence]
SPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFF
GLPQTGDLDQNTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGY
TPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDG
YPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGE
YCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFT
MGGNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGF
CPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANY
DDDRKWGFCPDQGYSLFLVAAHQFGHAMGLEHSQDPGALMAPIYTYTKNF
RLSQDDIKGIQELYGASP
3D structure
PDB1eak Crystal Structure of Human Mmp-2 Reveals a New P
ChainC
Resolution2.66 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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.
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 ZN C H178 D180 H193 H206 H147 D149 H162 H175
BS02 ZN C C102 H403 H407 H413 C71 H372 H376 H382
BS03 CA C D185 G186 D188 L190 D208 E211 D154 G155 D157 L159 D177 E180
BS04 CA C D168 G200 G202 D137 G169 G171
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1eak, PDBe:1eak, PDBj:1eak
PDBsum1eak
PubMed
UniProtP08253|MMP2_HUMAN 72 kDa type IV collagenase (Gene Name=MMP2)

[Back to BioLiP]