PDB ID: 4HN4
Hetero Atom Contents
color scheme of protein:
hetatm:
chain: Hide other chain(s)
Code | Name | Link |
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0JO | 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid | PoSSuM |
BCN | Bicine | PoSSuM |
CS | Cesium ion | PoSSuM |
F9F | 2-({[4-(trifluoromethoxy)phenyl]sulfonyl}amino)ethyl dihydrogen phosphate | PoSSuM |
PEG | Di(hydroxyethyl)ether | PoSSuM |
Download interaction data: 4HN4
Structure summary
Code : | 4HN4 PDBj RCSB PDB PDBe | ||||||||||||||||||||||||
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Header : | LYASE/LYASE INHIBITOR | ||||||||||||||||||||||||
Title : | Tryptophan synthase in complex with alpha aminoacrylate E(A-A) form and the F9 inhibitor in the alpha site | ||||||||||||||||||||||||
Release Data : | 2013-12-25 | ||||||||||||||||||||||||
Compound : |
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Source : |
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Authors : | Hilario, E., Niks, D., Dunn, M.F., Mueller, L.J., Fan, L. | ||||||||||||||||||||||||
Keywords : | Lyase, carbon-oxygen lyase, tryptophan biosynthesis, Salmonella, F9F, Allosteric enzyme, Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Pyridoxal phosphate, alpha amino acrylate, LYASE-LYASE INHIBITOR complex | ||||||||||||||||||||||||
Exp. method : | X-RAY DIFFRACTION ( 1.6400 Å ) | ||||||||||||||||||||||||
Citation : |
Allostery and substrate channeling in the tryptophan synthase bienzyme complex: evidence for two subunit conformations and four quaternary states.
Niks, D.,Hilario, E.,Dierkers, A.
et al.
PubMed: 23952479 |
Reaction
Chain : | A |
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UniProt : | P00929 (TRPA_SALTY) |
Reaction : | Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D- glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; Evidence={ECO:0000255|HAMAP-Rule:MF_00131}; |
Chain : | B |
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UniProt : | P0A2K1 (TRPB_SALTY) |
Reaction : | Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D- glyceraldehyde 3-phosphate + H2O + L-tryptophan; Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20; |