Structure of PDB 4dqw Chain A

Receptor sequence
>4dqwA (length=415) Species: 208964 (Pseudomonas aeruginosa PAO1) [Search protein sequence]
MLRISQEALTFDDVLLIPGYSEVLPKDVSLKTRLTRGIELNIPLVSAAMD
TVTEARLAIAMAQEGGIGIIHKNMGIEQQAAEVRKVKKHETAIVRDPVTV
TPSTKIIELLQMAREYGFSGFPVVEQGELVGIVTGRDLRVKPNAGDTVAA
IMTPKDKLVTAREGTPLEEMKAKLYENRIEKMLVVDENFYLRGLVTFRDI
EKAKTYPLASKDEQGRLRVGAAVGTGADTGERVAALVAAGVDVVVVDTAH
GHSKGVIERVRWVKQTFPDVQVIGGNIATAEAAKALAEAGADAVKVGIGP
GSICTTRIVAGVGVPQISAIANVAAALEGTGVPLIADGGIRFSGDLAKAM
VAGAYCVMMGSMFAGTEEAPGEPYKGALSAIVHQLMGGLRAAMGYTGSAD
IQQMRTQPQFVRITG
3D structure
PDB4dqw MgATP Regulates Allostery and Fiber Formation in IMPDHs.
ChainA
Resolution2.51 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.1.1.205: IMP 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 ATP A T134 R136 D137 T153 L158 V159 I179 E180 K181 T134 R136 D137 T153 L158 V159 I179 E180 K181
BS02 ATP A P97 V98 F118 E180 K181 L194 T196 R198 D199 P97 V98 F118 E180 K181 L194 T196 R198 D199
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0003938 IMP dehydrogenase activity
GO:0005524 ATP binding
GO:0016491 oxidoreductase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006177 GMP biosynthetic process
GO:0006183 GTP biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4dqw, PDBe:4dqw, PDBj:4dqw
PDBsum4dqw
PubMed23643948
UniProtQ9HXM5

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