Structure of PDB 1ps6 Chain A

Receptor sequence
>1ps6A (length=328) Species: 562 (Escherichia coli) [Search protein sequence]
VKTQRVVITPGEPAGIGPDLVVQLAQREWPVELVVCADATLLTNRAAMLG
LPLTLRPYSPNSPAQPQTAGTLTLLPVALRAPVTAGQLAVENGHYVVETL
ARACDGCLNGEFAALITGPVHKGVINDAGIPFTGHTEFFEERSQAKKVVM
MLATEELRVALATTHLPLRDIADAITPALLHEVIAILHHDLRTKFGIAEP
RILVCGLNPHAGEGGHMGTEEIDTIIPVLNELRAQGMKLNGPLPADTLFQ
PKYLDNADAVLAMYHDQGLPVLKYQGFGRGVNITLGLPFIRTSVDHGTAL
ELAGRGKADVGSFITALNLAIKMIVNTQ
3D structure
PDB1ps6 Crystal Structure of Escherichia coli PdxA, an Enzyme Involved in the Pyridoxal Phosphate Biosynthesis Pathway
ChainA
Resolution2.25 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.1.1.262: 4-hydroxythreonine-4-phosphate dehydrogenase.
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 ZN A H166 H266 H165 H265
BS02 4TP A H136 T137 H166 H266 N283 R292 H135 T136 H165 H265 N282 R291
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0008270 zinc ion binding
GO:0016491 oxidoreductase activity
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0050570 4-hydroxythreonine-4-phosphate dehydrogenase activity
GO:0050897 cobalt ion binding
GO:0051287 NAD binding
Biological Process
GO:0008615 pyridoxine biosynthetic process
GO:0042823 pyridoxal phosphate biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1ps6, PDBe:1ps6, PDBj:1ps6
PDBsum1ps6
PubMed12896974
UniProtP19624|PDXA_ECOLI 4-hydroxythreonine-4-phosphate dehydrogenase (Gene Name=pdxA)

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