Structure of PDB 1ho4 Chain C

Receptor sequence
>1ho4C (length=242) Species: 562 (Escherichia coli) [Search protein sequence]
AELLLGVNIDHIATLRNARGTAYPDPVQAAFIAEQAGADGITVHLREDRR
HITDRDVRILRQTLDTRMNLEMAVTEEMLAIAVETKPHFCCLVPEKRQEV
TTEGGLDVAGQRDKMRDACKRLADAGIQVSLFIDADEEQIKAAAEVGAPF
IEIHTGCYADAKTDAEQAQELARIAKAATFAASLGLKVNAGHGLTYHNVK
AIAAIPEMHELNIGHAIIGRAVMTGLKDAVAEMKRLMLEARG
3D structure
PDB1ho4 Structural basis for the function of pyridoxine 5'-phosphate synthase.
ChainC
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N9 H12 H45 R47 R51 E72 T103 E153 H193
Catalytic site (residue number reindexed from 1) N8 H11 H44 R46 R50 E71 T102 E152 H192
Enzyme Commision number 2.6.99.2: pyridoxine 5'-phosphate synthase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 PO4 C D11 H12 R47 H52 T102 D10 H11 R46 H51 T101
BS02 PXP C E72 T103 F133 E153 H193 G194 N213 I214 G215 H216 E71 T102 F132 E152 H192 G193 N212 I213 G214 H215
Gene Ontology
Molecular Function
GO:0016740 transferase activity
GO:0016769 transferase activity, transferring nitrogenous groups
GO:0033856 pyridoxine 5'-phosphate synthase activity
GO:0042802 identical protein binding
Biological Process
GO:0008615 pyridoxine biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ho4, PDBe:1ho4, PDBj:1ho4
PDBsum1ho4
PubMed11286891
UniProtP0A794|PDXJ_ECOLI Pyridoxine 5'-phosphate synthase (Gene Name=pdxJ)

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