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Ligands
Code Name Style Show Link
MIC Alpha-methylisocitric acid
SF4 Iron/sulfur cluster
Non-standard Residues
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Glycosylation
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Code : 1AMI   PDBj   RCSB PDB   PDBe
Header : LYASE(CARBON-OXYGEN)
Title : STERIC AND CONFORMATIONAL FEATURES OF THE ACONITASE MECHANISM
Release Data : 1995-01-26
Compound :
mol_id molecule chains
1 ACONITASE A
ec: 4.2.1.3
Source :
mol_id organism_scientific organism_common
1 Bos taurus  (taxid:9913) Cattle
Authors : Stout, C.D.
Keywords : LYASE(CARBON-OXYGEN)
Exp. method : X-RAY DIFFRACTION ( 2.0 Å )
Citation :

Steric and conformational features of the aconitase mechanism.

Lauble, H.,Stout, C.D.
(1995)  Proteins  22 : 1 - 11

PubMed: 7675781
DOI: 10.1002/prot.340220102

Crystal Structures of Aconitase with Trans-Aconitate and Nitrocitrate Bound

Lauble, H.,Kennedy, M.C.,Beinert, H.  et al.
(1994)  J.Mol.Biol.  237 : 437

Crystal Structures of Aconitase with Isocitrate and Nitroisocitrate Bound

Lauble, H.,Kennedy, M.C.,Beinert, H.  et al.
(1992)  Biochemistry  31 : 2735

Structure of Activated Aconitase. Formation of the (4Fe-4S) Cluster in the Crystal

Robbins, A.H.,Stout, C.D.
(1989)  Proc.Natl.Acad.Sci.USA  86 : 3639

The Structure of Aconitase

Robbins, A.H.,Stout, C.D.
(1989)  Proteins  5 : 289

Iron-Sulfur Cluster in Aconitase. Crystallographic Evidence for a Three-Iron Center

Robbins, A.H.,Stout, C.D.
(1985)  J.Biol.Chem.  260 : 2328

Chain : A
UniProt : P20004 (ACON_BOVIN)
Reaction: EC: Evidence:
Physiological Direction:
citrate = D-threo-isocitrate 4.2.1.3 UniProtKB:P19414
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