Brand  (β version)

PDB ID: 1GKM

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Ligands
Code Name Style Show Link
CYS Cysteine PoSSuM
GOL Glycerol PoSSuM
SO4 Sulfate ion PoSSuM
Non-standard Residues
Code Name Show
ZRF 2-[(4e)-2-[(1s)-1-aminoethyl]-4-(hydroxymethylidene)-5-oxo-4,5-dihydro-1h-imidazol-1-yl]acetic acid
Glycosylation
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Structure summary

Code : 1GKM   PDBj   RCSB PDB   PDBe
Header : LYASE
Title : HISTIDINE AMMONIA-LYASE (HAL) FROM PSEUDOMONAS PUTIDA INHIBITED WITH L-CYSTEINE
Release Data : 2002-04-05
Compound :
mol_id molecule chains synonym
1 Histidine ammonia-lyase B Histidase
ec: 4.3.1.3
mutation: YES
other_details: ALA 142, SER 143 AND GLY 144 ARE FORMING AN 4-METHYLIDENE-IMIDAZOLE-5-ONE GROUP(MDO). THE CARBONYL CARBON OF ALA 142 IS BONDED TO THE NITROGEN OF GLY 144. THE CARBONYL OXYGEN OF ALA 142 IS DELETED. THE SIDE CHAIN OF SER 143 IS DEHYDRATED.
Source :
mol_id organism_scientific expression_system
1 Pseudomonas putida  (taxid:303) ESCHERICHIA COLI  (taxid:469008)
gene: hutH
expression_system_strain: BL21(DE3)
expression_system_plasmid: PT7-7H
Authors : Baedeker, M., Schulz, G.E.
Keywords : LYASE, HISTIDINE DEGRADATION
Exp. method : X-RAY DIFFRACTION ( 1.0 Å )
Citation :

Structures of Two Histidine Ammonia-Lyase Modifications and Implications for the Catalytic Mechanism

Baedeker, M.,Schulz, G.E.
(2002)  Eur.J.Biochem.  269 : 1790

PubMed: 11895450
DOI: 10.1046/J.1432-1327.2002.02827.X

Crystal Structure of Histidine Ammonia-Lyase Revealing a Novel Polypeptide Modification as the Catalytic Electrophile

Schwede, T.F.,Retey, J.,Schulz, G.E.
(1999)  Biochemistry  38 : 5355

PubMed: 10220322
DOI: 10.1021/BI982929Q

Homogenization and Crystallization of Histidine Ammonia-Lyase by Exchange of a Surface Cysteine Residue

Schwede, T.F.,Baedeker, M.,Langer, M.  et al.
(1999)  Protein Eng.  12 : 151

PubMed: 10195286
DOI: 10.1093/PROTEIN/12.2.151

Reaction

Chain : B
UniProt : P21310 (HUTH_PSEPU)
Reaction: EC: Evidence:
Physiological Direction:
L-histidine = trans-urocanate + NH4(+) 4.3.1.3 PubMed:7947813, PubMed:8024588, PubMed:8204579, PubMed:8239649
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