Brand  (β version)

PDB ID: 1DE7

Hetero Atom Contents

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
NA Sodium ion PoSSuM
Non-standard Residues
Code Name Show
AR7 Amino{[(4s)-4-amino-5,5-dihydroxypentyl]amino}methaniminium
Glycosylation
Code Name Emphasize
Modification
Code Name Show
0QE Chloromethane

Structure summary

Code : 1DE7   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE SUBSTRATE
Title : INTERACTION OF FACTOR XIII ACTIVATION PEPTIDE WITH ALPHA-THROMBIN: CRYSTAL STRUCTURE OF THE ENZYME-SUBSTRATE COMPLEX
Release Data : 2000-12-13
Compound :
mol_id molecule chains
1 ALPHA-THROMBIN (LIGHT CHAIN) L,J
ec: 3.4.21.5
mol_id molecule chains
2 ALPHA-THROMBIN (HEAVY CHAIN) H,K
ec: 3.4.21.5
mol_id molecule chains
3 FACTOR XIII ACTIVATION PEPTIDE (28-37) A,B
Source :
mol_id organism_scientific organism_common
1 Homo sapiens  (taxid:9606) Human
tissue: PLASMA
mol_id organism_scientific organism_common
2 Homo sapiens  (taxid:9606) Human
tissue: PLASMA
mol_id organism_scientific
3
synthetic: yes
Authors : Sadasivan, C., Yee, V.C.
Keywords : ENZYME-SUBSTRATE COMPLEX, ALPHA-THROMBIN, FACTOR XIII ACTIVATION PEPTIDE, HYDROLASE/PEPTIDE, BLOOD CLOTTING, HYDROLASE-HYDROLASE SUBSTRATE complex
Exp. method : X-RAY DIFFRACTION ( 2.00 Å )
Citation :

Interaction of the factor XIII activation peptide with alpha -thrombin. Crystal structure of its enzyme-substrate analog complex.

Sadasivan, C.,Yee, V.C.
(2000)  J.Biol.Chem.  275 : 36942 - 36948

PubMed: 10956659
DOI: 10.1074/jbc.M006076200

The Refined 1.9 Angstroms X-Ray Crystal Structure of D-Phe-Pro-Arg Chloromethylketone-Inhibited Human Alpha-Thrombin: Structure Analysis, Overall Structure, Electrostatic Properties, Detailed Active-Site Geometry, and Structure-Function Relationships

Bode, W.,Turk, D.,Karshikov, A.
(1992)  Protein Sci.  1 : 426

The Interaction of Thrombin with Fibrinogen: A Structural Basis for its Specificity

Stubbs, M.T.,Oschkinat, H.,Mayer, I.  et al.
(1992)  Eur.J.Biochem.  206 : 187

Three-Dimensional Structure of a Transglutaminase: Human Blood Coagulation Factor Xiii

Yee, V.C.,Pedersen, L.C.,Trong, I.L.  et al.
(1994)  Proc.Natl.Acad.Sci.USA  91 : 7296

Reaction

Chain : H, K
UniProt : P00734 (THRB_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B. 3.4.21.5 -
-