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Ligands
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DPM 3-[5-{[3-(2-carboxyethyl)-4-(carboxymethyl)-5-methyl-1h-pyrrol-2-yl]methyl}-4-(carboxymethyl)-1h-pyrrol-3-yl]propanoic acid
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Code : 1YPN   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : REDUCED FORM HYDROXYMETHYLBILANE SYNTHASE (K59Q MUTANT) CRYSTAL STRUCTURE AFTER 2 HOURS IN A FLOW CELL DETERMINED BY TIME-RESOLVED LAUE DIFFRACTION
Release Data : 1999-03-02
Compound :
mol_id molecule chains synonym
1 HYDROXYMETHYLBILANE SYNTHASE A PORPHOBILINOGEN DEAMINASE
ec: 2.5.1.61
fragment: THREE DOMAINS
mutation: K59Q
other_details: CONTAINS A DIPYRROMETHANE COFACTOR LINKED TO CYSTEINE 242
Source :
mol_id organism_scientific expression_system
1 Escherichia coli  (taxid:562) Escherichia coli  (taxid:562)
Authors : Helliwell, J.R., Nieh, Y.P., Raftery, J., Cassetta, A., Habash, J., Carr, P.D., Ursby, T., Wulff, M., Thompson, A.W., Niemann, A.C., Haedener, A.
Keywords : BIOSYNTHESIS OF LINEAR TETRAPYRROLE, ALL ALPHA/BETA, TRANSFERASE
Exp. method : X-RAY DIFFRACTION ( 2.3 Å )
Citation :

Time-Resolved Structures of Hydroxymethylbilane Synthase (Lys59Gln Mutant) as It Isloaded with Substrate in the Crystal Determined by Laue Diffraction

Helliwell, J.R.,Nieh, Y.P.,Cassetta, A.  et al.
(1998)  J.Chem.Soc.,Faraday Trans.  94 : 2615 - 2622

DOI: 10.1039/A802217H

Time-Resolved Protein Crystal Diffraction: Determination by the Laue Method of the Behaviour of the Enzyme Hydroxymethylbilane Synthase (Lys59Gln Mutant) as It is Loaded with Substrate in the Crystal

Helliwell, J.R.,Nieh, Y.P.,Cassetta, A.  et al.
(1997)  Time-Resolved Diffraction (in: Oxford Series on Synchrotron Radiation, V.2)  : 187

Chain : A
UniProt : P06983 (HEM3_ECOLI)
Reaction: EC: Evidence:
Physiological Direction:
H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+) 2.5.1.61 PubMed:3052434
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