Structure of PDB 1eak Chain D

Receptor sequence

>1eakD (length=419) Species: 9606 (Homo sapiens)

SPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFF
GLPQTGDLDQNTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGY
TPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDG
YPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGE
YCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFT
MGGNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGF
CPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANY
DDDRKWGFCPDQGYSLFLVAAHQFGHAMGLEHSQDPGALMAPIYTYTKNF
RLSQDDIKGIQELYGASPD

3D structure

• PDB: 1eak Crystal Structure of Human Mmp-2 Reveals a New P
• Chain: D
• Resolution: 2.66 Å

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	peptide	D	P133 D209 H276 E277 A278 F293 S304	P102 D178 H245 E246 A247 F262 S273
BS02	ZN	D	H178 D180 H193 H206	H147 D149 H162 H175
BS03	ZN	D	C102 H403 H407 H413	C71 H372 H376 H382
BS04	CA	D	D185 G186 D188 L190 D208 E211	D154 G155 D157 L159 D177 E180
BS05	CA	D	A167 D168	A136 D137

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

External links

• PDB: RCSB:1eak, PDBe:1eak, PDBj:1eak
• PDBsum: 1eak
• UniProt: P08253|MMP2_HUMAN 72 kDa type IV collagenase (Gene Name=MMP2)