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3PDK

crystal structure of phosphoglucosamine mutase from B. anthracis

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004615molecular_functionphosphomannomutase activity
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006048biological_processUDP-N-acetylglucosamine biosynthetic process
A0008966molecular_functionphosphoglucosamine mutase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0016853molecular_functionisomerase activity
A0016868molecular_functionintramolecular phosphotransferase activity
A0046872molecular_functionmetal ion binding
A0071704biological_processorganic substance metabolic process
B0000287molecular_functionmagnesium ion binding
B0004615molecular_functionphosphomannomutase activity
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0006048biological_processUDP-N-acetylglucosamine biosynthetic process
B0008966molecular_functionphosphoglucosamine mutase activity
B0009252biological_processpeptidoglycan biosynthetic process
B0016853molecular_functionisomerase activity
B0016868molecular_functionintramolecular phosphotransferase activity
B0046872molecular_functionmetal ion binding
B0071704biological_processorganic substance metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 449
ChainResidue
AVAL306
AARG410
ASER412
AARG419

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 450
ChainResidue
AASP308
AMET312
AHIS329
ATHR338
AGLY339

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 A 451
ChainResidue
AHIS277
AHOH459

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 449
ChainResidue
BARG410
BSER412
BTHR414
BARG419

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 B 450
ChainResidue
ATHR202
AMET203
AGLY204
ATHR205
ASER206
BGLY364
BTHR367

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 451
ChainResidue
BASP308
BMET312
BHIS329
BILE331
BTHR338
BGLY339

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 B 452
ChainResidue
BHIS277
BHOH461

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 453
ChainResidue
BHIS101
BASN102
BPRO103
BTHR219

Functional Information from PROSITE/UniProt
site_idPS00710
Number of Residues10
DetailsPGM_PMM Phosphoglucomutase and phosphomannomutase phosphoserine signature. GVmISASHNP
ChainResidueDetails
AGLY94-PRO103

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Phosphoserine intermediate => ECO:0000255|HAMAP-Rule:MF_01554
ChainResidueDetails
ASER100
BSER100

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: via phosphate group => ECO:0000255|HAMAP-Rule:MF_01554
ChainResidueDetails
ASER100
BSER100

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01554
ChainResidueDetails
AASP240
AASP242
AASP244
BASP240
BASP242
BASP244

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000255|HAMAP-Rule:MF_01554
ChainResidueDetails
ASER100
BSER100

218853

PDB entries from 2024-04-24

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