Structure of PDB 2woe Chain B

Receptor sequence
>2woeB (length=291) Species: 1085 (Rhodospirillum rubrum) [Search protein sequence]
GPSVHDRALGAFLGLAVGDALGATVEFMTKGEIAQQYGIHRKMTGGGWLR
LKPGQITDDTEMSLALGRSLAAKGTLDVADICEEFALWLKSRPVNVGNTC
RRGIRRYMHEGTTTAPYSEGDAGNGAAMRCLPAALATLGHPADLEPWVLA
QARITHNHPLSDAACLTLGRMVHHLIGGRGMKACREEANRLVHQHRDFHF
EPYKGQSSAYIVDTMQTVLHYYFVTDTFKSCLIQTVNQGGDADTTGALAG
MLAGATYGVDDIPSGWLSKLDMKVEREIRRQVDALLALAGL
3D structure
PDB2woe Mechanism of Adp-Ribosylation Removal Revealed by the Structure and Ligand Complexes of the Dimanganese Mono-Adp-Ribosylhydrolase Drag.
ChainB
Resolution1.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.2.24: ADP-ribosyl-[dinitrogen reductase] hydrolase.
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 MN B E28 D243 D245 T246 E26 D241 D243 T244
BS02 AR6 B D60 N97 G99 N100 T101 G122 A124 G125 N126 G127 H158 A211 Y212 D243 D58 N95 G97 N98 T99 G120 A122 G123 N124 G125 H156 A209 Y210 D241
BS03 AR6 B D273 K275 D271 K273
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
GO:0047407 ADP-ribosyl-[dinitrogen reductase] hydrolase activity
Biological Process
GO:0009399 nitrogen fixation
GO:0051725 protein de-ADP-ribosylation
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:2woe, PDBe:2woe, PDBj:2woe
PDBsum2woe
PubMed19706507
UniProtP14300|DRAG_RHORU ADP-ribosyl-[dinitrogen reductase] glycohydrolase (Gene Name=draG)

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