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3UWZ

Crystal structure of Staphylococcus aureus triosephosphate isomerase complexed with glycerol-2-phosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004807molecular_functiontriose-phosphate isomerase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0019563biological_processglycerol catabolic process
A0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
B0004807molecular_functiontriose-phosphate isomerase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016853molecular_functionisomerase activity
B0019563biological_processglycerol catabolic process
B0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE G2H A 254
ChainResidue
ALYS11
AGLY213
ASER215
AGLY236
AGLY237
AHOH255
AHOH275
AHOH280
AHOH296

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 255
ChainResidue
BMET225
BGLN227
BTHR228
BILE230
BASP231
BHOH282

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE G2H B 254
ChainResidue
BLYS11
BSER215
BLYS217
BGLY236
BGLY237
BHOH305
BHOH317

Functional Information from PROSITE/UniProt
site_idPS00171
Number of Residues11
DetailsTIM_1 Triosephosphate isomerase active site. AYEPIWAIGTG
ChainResidueDetails
AALA167-GLY177

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Electrophile => ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000305|PubMed:22813930
ChainResidueDetails
AHIS97
BHIS97

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000305|PubMed:22813930
ChainResidueDetails
AGLU169
BGLU169

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000269|PubMed:22813930
ChainResidueDetails
AASN9
AGLY175
ASER215
AGLY236
BASN9
BGLY175
BSER215
BGLY236

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PDB entries from 2024-08-28

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