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2IFY

Structure of Bacillus anthracis cofactor-independent phosphoglucerate mutase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004619molecular_functionphosphoglycerate mutase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006007biological_processglucose catabolic process
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0030145molecular_functionmanganese ion binding
A0030435biological_processsporulation resulting in formation of a cellular spore
A0043937biological_processregulation of sporulation
A0046537molecular_function2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN A 601
ChainResidue
AASP402
AHIS406
AHIS461
AHOH716

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN A 701
ChainResidue
AASP11
ASER61
AASP443
AHIS444

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Phosphoserine intermediate => ECO:0000269|PubMed:17085493
ChainResidueDetails
ASER61

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:17085493
ChainResidueDetails
AASP11
ASER61
AASP402
AHIS406
AASP443
AHIS444
AHIS461

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01038
ChainResidueDetails
AHIS122
AARG152
AARG184
AARG190
AARG260
ALYS335

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000255|HAMAP-Rule:MF_01038
ChainResidueDetails
ATYR35

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1o98
ChainResidueDetails
ASER61
AARG260
AASP153

222036

PDB entries from 2024-07-03

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