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Ligands
Code Name Style Show Link
29P 3-[(5s)-5-{[3-(2-carboxyethyl)-4-(carboxymethyl)-5-methyl-1h-pyrrol-2-yl]methyl}-4-(carboxymethyl)-2-oxo-2,5-dihydro-1h-pyrrol-3-yl]propanoic acid
ACY Acetic acid
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 : 4MLV   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : Crystal Structure of Bacillus megaterium porphobilinogen deaminase
Release Data : 2014-04-02
Compound :
mol_id molecule chains synonym
1 Porphobilinogen deaminase A PBG, Hydroxymethylbilane synthase, Pre-uroporphyrinogen synthase
ec: 2.5.1.61
fragment: porphobilinogen deaminase
Source :
mol_id organism_scientific expression_system
1 Bacillus megaterium  (taxid:1404) Escherichia coli  (taxid:562)
gene: hemC
expression_system_strain: Rosetta DE3
expression_system_vector_type: plasmid
expression_system_plasmid: pET14b
Authors : Azim, N., Deery, E., Warren, M.J., Erskine, P., Cooper, J.B., Coker, A., Wood, S.P., Akhtar, M.
Keywords : Tetrapyrrole biosynthesis, porphobilinogen deaminase, dipyrromethane cofactor, three-domain fold, domains 1 and 2 resemble the fold of type II periplasmic binding proteins, pyrrole polymerisation, TRANSFERASE
Exp. method : X-RAY DIFFRACTION ( 1.455 Å )
Citation :

Structural evidence for the partially oxidized dipyrromethene and dipyrromethanone forms of the cofactor of porphobilinogen deaminase: structures of the Bacillus megaterium enzyme at near-atomic resolution.

Azim, N.,Deery, E.,Warren, M.J.  et al.
(2014)  Acta Crystallogr.,Sect.D  70 : 744 - 751

PubMed: 24598743
DOI: 10.1107/S139900471303294X

Chain : A
UniProt : Q8GCA8 (Q8GCA8_PRIMG)
Reaction: EC: Evidence:
Physiological Direction:
H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+) 2.5.1.61 ARBA:ARBA00000416, HAMAP- Rule:MF_00260
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