Structure of PDB 4qax Chain A Binding Site BS01

Receptor Information
>4qax Chain A (length=503) Species: 93061 (Staphylococcus aureus subsp. aureus NCTC 8325) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KKPTALIILDGFANRESEHGNAVKLANKPNFDRYYNKYPTTQIEASGLDV
GLPEGQMGNSEVGHMNIGAGRIVYQSLTRINKSIEDGDFFENDVLNNAIA
HVNSHDSALHIFGLLSDGGVHSHYKHLFALLELAKKQGVEKVYVHAFLDG
RDVDQKSALKYIEETEAKFNELGIGQFASVSGRYYAMDRDKRWEREEKAY
NAIRNFDAPTYATAKEGVEASYNEGLTDEFVVPFIVENQNDGVNDGDAVI
FYNFRPDRAAQLSEIFANRAFEGFKVEQVKDLFYATFTKYNDNIDAAIVF
EKVDLNNTIGEIAQNNNLTQLRIAETEKYPHVTYFMSGGRNEEFKGERRR
LIDSPKVATYDLKPEMSAYEVKDALLEELNKGDLDLIILNFANPDMVGHS
GMLEPTIKAIEAVDECLGEVVDKILDMDGYAIITADHGNSDQVLTDDDQP
MTTHTTNPVPVIVTKEGVTLRETGRLGDLAPTLLDLLNVEQPEDMTGESL
IKH
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain4qax Chain A Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB4qax STRUCTURAL AND FUNCCTIONAL ANALYSIS of PHOSPHOGLYCERATE MUTASE from STAPHYLOCOCCUS AUREUS
Resolution2.0 Å
Binding residue
(original residue number in PDB)		D397 H401 H456
Binding residue
(residue number reindexed from 1)		D395 H399 H454
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D12 S62 D154 R257 K330 D397 H401 D438 H439 H456
Catalytic site (residue number reindexed from 1) D10 S60 D152 R255 K328 D395 H399 D436 H437 H454
Enzyme Commision number 5.4.2.12: phosphoglycerate mutase (2,3-diphosphoglycerate-independent).
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004619 phosphoglycerate mutase activity
GO:0016853 isomerase activity
GO:0030145 manganese ion binding
GO:0046537 2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006007 glucose catabolic process
GO:0006096 glycolytic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4qax, PDBe:4qax, PDBj:4qax
PDBsum4qax
PubMed
UniProtQ2G029

[Back to BioLiP]