Structure of PDB 4g3h Chain D

Receptor sequence
>4g3hD (length=300) Species: 85962 (Helicobacter pylori 26695) [Search protein sequence]
MILVGLEAELGASKRGTDKGVRRLREALSATHGDVIKGMQTITQERCVLY
KEFRYAKNFEDYYLFCKENLIPCMKEVFEKKEFPLILSSEHANMFGIFQA
FRSVHKDKKIGILYLDAHADIHTAIHGMPLGMVLNRVRSMSESEEKAWQK
LCSLGLEKGGLEIDPKCLVYFGVRSTEQSERDVIRELQIPLFSVDAIREN
MQEVVQKTKESLKAVDIIYLSLDLDIMDGKLFTSTGVRENNGLSFDELKQ
LLGLLLESFKDRLKAVEVTEYNPTVSIKHNNEEEKQVLEILDLIINSCKI
3D structure
PDB4g3h Structure and function studies on Helicobacter pylori arginase
ChainD
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H91 D116 H118 D120 H133 D234 D236 E281
Catalytic site (residue number reindexed from 1) H91 D116 H118 D120 H126 D223 D225 E270
Enzyme Commision number 3.5.3.1: arginase.
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 D H91 D116 D120 D234 H91 D116 D120 D223
BS02 MN D D116 H118 D234 D236 D116 H118 D223 D225
Gene Ontology
Molecular Function
GO:0004053 arginase activity
GO:0016787 hydrolase activity
GO:0016813 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
GO:0030145 manganese ion binding
GO:0046872 metal ion binding
Biological Process
GO:0006525 arginine metabolic process
GO:0019547 arginine catabolic process to ornithine
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:4g3h, PDBe:4g3h, PDBj:4g3h
PDBsum4g3h
PubMed
UniProtO25949

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