Structure of PDB 4g3h Chain A Binding Site BS02

Receptor Information

>4g3h Chain A (length=301) Species: 85962 (Helicobacter pylori 26695)

MILVGLEAELGASKRGTDKGVRRLREALSATHGDVIKGMQTITQERCVLY
KEFRYAKNFEDYYLFCKENLIPCMKEVFEKKEFPLILSSEHANMFGIFQA
FRSVHKDKKIGILYLDAHADIHTAYIHGMPLGMVLNRVRRMSESEEKAWQ
KLCSLGLEKGGLEIDPKCLVYFGVRSTEQSERDVIRELQIPLFSVDAIRE
NMQEVVQKTKESLKAVDIIYLSLDLDIMDGKLFTSTGVRENNGLSFDELK
QLLGLLLESFKDRLKAVEVTEYNPTVSIKHNNEEEKQVLEILDLIINSCK
I

Ligand information

• Ligand ID: MN
• InChI: InChI=1S/Mn/q+2
• InChIKey: WAEMQWOKJMHJLA-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mn+2]
  CACTVS 3.341: [Mn++]
• Formula: Mn
• Name: MANGANESE (II) ION
• DrugBank: DB06757
• PDB chain: 4g3h Chain A Residue 501

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4g3h Structure and function studies on Helicobacter pylori arginase
• Resolution: 2.2 Å
• Binding residue (original residue number in PDB): D116 H118 D234 D236
• Binding residue (residue number reindexed from 1): D116 H118 D224 D226
• Annotation score: 1

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 H127 D224 D226 E271
• Enzyme Commision number: 3.5.3.1: arginase.

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

External links

• PDB: RCSB:4g3h, PDBe:4g3h, PDBj:4g3h
• PDBsum: 4g3h
• UniProt: O25949