Structure of PDB 4nwx Chain A

Receptor sequence
>4nwxA (length=503) Species: 93061 (Staphylococcus aureus subsp. aureus NCTC 8325) [Search protein sequence]
KKPTALIILDGFANRESEHGNAVKLANKPNFDRYYNKYPTTQIEASGLDV
GLPEGQMGNSEVGHMNIGAGRIVYQSLTRINKSIEDGDFFENDVLNNAIA
HVNSHDSALHIFGLLSDGGVHSHYKHLFALLELAKKQGVEKVYVHAFLDG
RDVDQKSALKYIEETEAKFNELGIGQFASVSGRYYAMDRDKRWEREEKAY
NAIRNFDAPTYATAKEGVEASYNEGLTDEFVVPFIVENQNDGVNDGDAVI
FYNFRPDRAAQLSEIFANRAFEGFKVEQVKDLFYATFTKYNDNIDAAIVF
EKVDLNNTIGEIAQNNNLTQLRIAETEKYPHVTYFMSGGRNEEFKGERRR
LIDSPKVATYDLKPEMSAYEVKDALLEELNKGDLDLIILNFANPDMVGHS
GMLEPTIKAIEAVDECLGEVVDKILDMDGYAIITADHGNSDQVLTDDDQP
MTTHTTNPVPVIVTKEGVTLRETGRLGDLAPTLLDLLNVEQPEDMTGESL
IKH
3D structure
PDB4nwx Complete catalytic cycle of cofactor-independent phosphoglycerate mutase involves a spring-loaded mechanism
ChainA
Resolution2.01 Å
3D
structure
Catalytic site residues are labeled in the structure
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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).
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 2PG A H123 D154 R185 R191 R257 R260 H121 D152 R183 R189 R255 R258
BS02 MN A D12 S62 D438 H439 D10 S60 D436 H437
BS03 MN A D397 H401 H456 D395 H399 H454
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4nwx, PDBe:4nwx, PDBj:4nwx
PDBsum4nwx
PubMed25611430
UniProtQ2G029

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