Structure of PDB 1vbh Chain A

Receptor sequence
>1vbhA (length=862) Species: 4577 (Zea mays) [Search protein sequence]
KKRVFHFGKGKSEGNKTMKELLGGKGANLAEMASIGLSVPPGFTVSTEAC
QQYQDAGCALPAGLWAEIVDGLQWVEEYMGATLGDPQRPLLLSVRSGAAV
SMPGMMDTVLNLGLNDEVAAGLAAKSGERFAYDSFRRFLDMFGNVVMDIP
RSLFEEKLEHMKESKGLKNDTDLTASDLKELVGQYKEVYLSAKGEPFPSD
PKKQLELAVLAVFNSWESPRAKKYRSINQITGLRGTAVNVQCMVFGNMGN
TSGTGVLFTRNPNTGEKKLYGEFLVNARTPEDLDAMKNLMPQAYDELVEN
CNILESHYKEMQDIEFTVQENRLWMLQCRTGKRTGKSAVKIAVDMVNEGL
VEPRSAIKMVEPGHLDQLLHPQFENPSAYKDQVIATGLPASPGAAVGQVV
FTAEDAEAWHSQGKAAILVRAETSPEDVGGMHAAVGILTEMTSHAAVVAR
GWGKCCVSGCSGIRVNDAEKLVTIGGHVLREGEWLSLNGSTGEVILGKQP
LSPPALSGDLGTFMAWVDDVRKLKVLANADTPDDALTARNNGAQGIGLCR
TEHMFFASDERIKAVRQMIMAPTLELRQQALDRLLPYQRSDFEGIFRAMD
GLPVTIRLLDPPLHEFLPEGNIEDIVSELCAETGANQEDALARIEKLSEV
NPMLGFRGCRLGISYPELTEMQARAIFEAAIAMTNQGVQVFPEIMVPLVG
TPQELGHQVTLIRQVAEKVFANVGKTIGYKVGTMIEIPRAALVADEIAEQ
AEFFSFGTNDLTQMTFGYSRDDVGKFIPVYLAQGILQHDPFEVLDQRGVG
ELVKFATERGRKARPNLKVGICGEHGGEPSSVAFFAKAGLDYVSCSPFRV
PIARLAAAQVLV
3D structure
PDB1vbh Crystal structures of pyruvate phosphate dikinase from maize revealed an alternative conformation in the swiveling-domain motion
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) K27 R97 G106 M108 R340 H458 E750 S769 D774 C836 Y856
Catalytic site (residue number reindexed from 1) K25 R95 G104 M106 R329 H444 E736 S755 D760 C822 Y842
Enzyme Commision number 2.7.9.1: pyruvate, phosphate dikinase.
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 MG A E750 D774 E736 D760
BS02 PEP A R564 R621 G771 N773 D774 C836 G837 R550 R607 G757 N759 D760 C822 G823
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0016772 transferase activity, transferring phosphorus-containing groups
GO:0046872 metal ion binding
GO:0050242 pyruvate, phosphate dikinase activity
Biological Process
GO:0006090 pyruvate metabolic process
GO:0015979 photosynthesis
GO:0016310 phosphorylation
Cellular Component
GO:0005737 cytoplasm
GO:0009507 chloroplast

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1vbh, PDBe:1vbh, PDBj:1vbh
PDBsum1vbh
PubMed15667207
UniProtP11155|PPDK1_MAIZE Pyruvate, phosphate dikinase 1, chloroplastic (Gene Name=PPDK1)

[Back to BioLiP]