PDBsum entry: 1eak

Hydrolase/hydrolase inhibitor

PDB id: 1eak

Contents

Protein chains

421 a.a. *

Ligands

GLY-PRO-ALA-GLY-PRO-PRO-GLY-ALA ×2

SO4 ×6

Metals

_CA ×8

_ZN ×8

Waters ×109

* Residue conservation analysis

PDB id:

1eak

Name:

Hydrolase/hydrolase inhibitor

Title:

Catalytic domain of prommp-2 e404q mutant

Structure:

72 kda type iv collagenase. Chain: a, b, c, d. Fragment: catalytic domain residues 32-452. Synonym: gelatinase a, 72 kda gelatinase, matrix metalloproteinase-2, mmp-2. Engineered: yes. Mutation: yes. Inhibitor peptide. Chain: p, r.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Expression_system_cell_line: high 5. Synthetic: yes

Biol. unit:

Trimer (from PDB file)

Resolution:

2.66Å R-factor: 0.271 R-free: 0.303

Authors:

U.Bergmann,A.Tuuttila,K.Tryggvason,E.Morgunova

Key ref:

U.Bergmann et al. Crystal structure of human mmp-2 reveals a new p. To be published,

Date:

12-Jul-01 Release date: 22-Aug-02

Protein chains

P08253  (MMP2_HUMAN) -  72 kDa type IV collagenase

Seq: 660 a.a.

Struc: 421 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.3.4.24.24 - Gelatinase A.
• Reaction: Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.
• Cofactor: Calcium; Zinc

 Gene Ontology (GO) functional annotation 

• Cellular component: extracellular matrix (1 term)
• Biological process: metabolic process (2 terms)
• Biochemical function: metallopeptidase activity (3 terms)