PDBsum entry: 1a2c

Hydrolase/hydrolase inhibitor

PDB id: 1a2c

Contents

Protein chains

36 a.a. *

252 a.a. *

Ligands

ASP-PHE-GLU-GLU-ILE-PRO-GLU-GLU-TYS-LEU

34H-LEU-PRJ-OAR

Metals

_NA

Waters ×176

* Residue conservation analysis

PDB id:

1a2c

Name:

Hydrolase/hydrolase inhibitor

Title:

Structure of thrombin inhibited by aeruginosin298-a from a b alga

Structure:

Thrombin light chain. Chain: l. Thrombin heavy chain. Chain: h. Hirudin variant-2. Chain: i. Fragment: unp residues 60-71. Engineered: yes. Aeruginosin 298-a.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Microcystis aeruginosa. Organism_taxid: 1126

Biol. unit:

Tetramer (from PQS)

Resolution:

2.10Å R-factor: 0.150

Authors:

J.L.Rios-Steiner,M.Murakami,A.Tulinsky

Key ref:

J.L.R.Steiner et al. (1998). Structure of thrombin inhibited by aeruginosin 298-A from a blue-Green alga. J.Am.Chem.Soc., 120,

Date:

26-Dec-97 Release date: 01-Jul-98

Protein chain

P00734  (THRB_HUMAN) -  Prothrombin

Seq: 622 a.a.

Struc: 36 a.a.

Protein chain

P00734  (THRB_HUMAN) -  Prothrombin

Seq: 622 a.a.

Struc: 252 a.a.

Enzyme reactions

• Enzyme class: Chains L, H: E.C.3.4.21.5 - Thrombin.
• Reaction: Preferential cleavage: Arg-|-Gly; activates fibrinogen to fibrin and releases fibrinopeptide A and B.

 Gene Ontology (GO) functional annotation 

• Cellular component: extracellular region (1 term)
• Biological process: blood coagulation (2 terms)
• Biochemical function: catalytic activity (3 terms)