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3LNT

Crystal structure of phosphoglyceromutase from Burkholderia Pseudomallei 1710B with bound malonic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004619molecular_functionphosphoglycerate mutase activity
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0016868molecular_functionintramolecular phosphotransferase activity
A0046538molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
B0003824molecular_functioncatalytic activity
B0004619molecular_functionphosphoglycerate mutase activity
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016853molecular_functionisomerase activity
B0016868molecular_functionintramolecular phosphotransferase activity
B0046538molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 250
ChainResidue
ATRP23
AHOH252
AHOH259
AHOH284

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE MLI A 990
ChainResidue
AGLY22
AGLU87
ATYR90
AHOH255
AHOH268
AHOH300
AHOH304
AHOH360
AARG8
AHIS9
AASN15
AARG19
ATHR21

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE MLI B 990
ChainResidue
BARG8
BHIS9
BASN15
BARG19
BTHR21
BGLY22
BGLU87
BTYR90
BHOH273
BHOH322
BHOH327
BHOH359

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 250
ChainResidue
AEDO251
BARG63
BTRP66
BHIS67

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 251
ChainResidue
AARG63
AHIS67
BEDO250

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 251
ChainResidue
AVAL79
AHOH260
BPRO78
BVAL79
BARG115
BHOH289

Functional Information from PROSITE/UniProt
site_idPS00175
Number of Residues10
DetailsPG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LiRHGEsTwN
ChainResidueDetails
ALEU6-ASN15

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Tele-phosphohistidine intermediate => ECO:0000255|HAMAP-Rule:MF_01039, ECO:0000269|PubMed:21904048
ChainResidueDetails
AHIS9
BHIS9

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_01039
ChainResidueDetails
AGLU87
BGLU87

site_idSWS_FT_FI3
Number of Residues28
DetailsBINDING: BINDING => ECO:0000269|PubMed:21904048, ECO:0007744|PDB:3FDZ
ChainResidueDetails
AARG8
AARG114
AARG115
AHIS182
AGLY183
AASN184
BARG8
BHIS9
BASN15
BTHR21
BGLY22
AHIS9
BARG60
BGLU87
BTYR90
BLYS98
BARG114
BARG115
BHIS182
BGLY183
BASN184
AASN15
ATHR21
AGLY22
AARG60
AGLU87
ATYR90
ALYS98

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01039
ChainResidueDetails
AHIS182
BHIS182

223532

PDB entries from 2024-08-07

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