Structure of PDB 4g3h Chain D Binding Site BS01
Receptor Information
>4g3h Chain D (length=300) Species:
85962
(Helicobacter pylori 26695) [
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MILVGLEAELGASKRGTDKGVRRLREALSATHGDVIKGMQTITQERCVLY
KEFRYAKNFEDYYLFCKENLIPCMKEVFEKKEFPLILSSEHANMFGIFQA
FRSVHKDKKIGILYLDAHADIHTAIHGMPLGMVLNRVRSMSESEEKAWQK
LCSLGLEKGGLEIDPKCLVYFGVRSTEQSERDVIRELQIPLFSVDAIREN
MQEVVQKTKESLKAVDIIYLSLDLDIMDGKLFTSTGVRENNGLSFDELKQ
LLGLLLESFKDRLKAVEVTEYNPTVSIKHNNEEEKQVLEILDLIINSCKI
Ligand information
Ligand ID
MN
InChI
InChI=1S/Mn/q+2
InChIKey
WAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341
[Mn++]
Formula
Mn
Name
MANGANESE (II) ION
ChEMBL
DrugBank
DB06757
ZINC
PDB chain
4g3h Chain D Residue 500 [
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Receptor-Ligand Complex Structure
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PDB
4g3h
Structure and function studies on Helicobacter pylori arginase
Resolution
2.2 Å
Binding residue
(original residue number in PDB)
H91 D116 D120 D234
Binding residue
(residue number reindexed from 1)
H91 D116 D120 D223
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 H126 D223 D225 E270
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
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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
PDBsum
4g3h
PubMed
UniProt
O25949
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