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5T73

Crystal structure of S.aureus glyceraldehyde-3-phosphate-dehydrogenase (Gap) containing oxidized Cys151

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
A0005737cellular_componentcytoplasm
A0006006biological_processglucose metabolic process
A0006096biological_processglycolytic process
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
B0000166molecular_functionnucleotide binding
B0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
B0005737cellular_componentcytoplasm
B0006006biological_processglucose metabolic process
B0006096biological_processglycolytic process
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0050661molecular_functionNADP binding
B0051287molecular_functionNAD binding
C0000166molecular_functionnucleotide binding
C0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
C0005737cellular_componentcytoplasm
C0006006biological_processglucose metabolic process
C0006096biological_processglycolytic process
C0016491molecular_functionoxidoreductase activity
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0050661molecular_functionNADP binding
C0051287molecular_functionNAD binding
D0000166molecular_functionnucleotide binding
D0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
D0005737cellular_componentcytoplasm
D0006006biological_processglucose metabolic process
D0006096biological_processglycolytic process
D0016491molecular_functionoxidoreductase activity
D0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D0050661molecular_functionNADP binding
D0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue NA A 401
ChainResidue
AASP34
ATHR36
AASP38
APHE75
ASER76

site_idAC2
Number of Residues4
Detailsbinding site for residue NA A 402
ChainResidue
AILE21
AVAL24
ALEU27
AHOH530

site_idAC3
Number of Residues7
Detailsbinding site for residue NA B 401
ChainResidue
BASP34
BTHR36
BASP38
BLEU41
BPHE75
BSER76
BHOH534

site_idAC4
Number of Residues5
Detailsbinding site for residue NA B 402
ChainResidue
BILE21
BVAL24
BLEU27
BHOH541
BHOH542

site_idAC5
Number of Residues6
Detailsbinding site for residue NA C 401
ChainResidue
CASP34
CTHR36
CASP38
CPHE75
CSER76
CHOH532

site_idAC6
Number of Residues6
Detailsbinding site for residue NA C 402
ChainResidue
CILE21
CGLN22
CVAL24
CLEU27
CGLU28
CHOH538

site_idAC7
Number of Residues7
Detailsbinding site for residue NA D 401
ChainResidue
DASP34
DTHR36
DASP38
DSER74
DPHE75
DSER76
DHOH516

site_idAC8
Number of Residues4
Detailsbinding site for residue NA D 402
ChainResidue
DILE21
DVAL24
DLEU27
DHOH544

Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNsL
ChainResidueDetails
AALA149-LEU156

site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. MSVGDRQLVKVAAWY
ChainResidueDetails
AMET300-TYR314

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"20620151","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20620151","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of Staphylococcal GAPDH1 in a hexagonal space group.","authors":["Roychowdhury A.","Mukherjee S.","Dutta D.","Das A.K."]}}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20620151","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00362","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsSite: {"description":"Activates thiol group during catalysis","evidences":[{"source":"PubMed","id":"20620151","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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