Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6OK4

Crystal Structure of Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Chlamydia trachomatis with bound NAD

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 Residues27
Detailsbinding site for residue NAD A 401
ChainResidue
AGLY7
ATHR96
AGLY97
ALEU98
ATHR119
AALA120
ACYS150
AALA181
AASN314
ATYR318
AHOH507
APHE8
AHOH519
AHOH538
AHOH543
AHOH549
AHOH561
AHOH571
AHOH576
CHOH514
AGLY9
AARG10
AILE11
AASN32
AASP33
ALEU34
ASER95

site_idAC2
Number of Residues2
Detailsbinding site for residue EDO A 402
ChainResidue
ATHR128
AASN134

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 403
ChainResidue
ALYS246
AHOH539
BGLU170
CARG304
CEDO404

site_idAC4
Number of Residues8
Detailsbinding site for residue PO4 A 404
ChainResidue
ASER149
ATHR151
ATHR209
AGLY210
AALA211
AHOH509
AHOH530
AHOH537

site_idAC5
Number of Residues8
Detailsbinding site for residue PO4 A 405
ChainResidue
AGLU170
ALYS246
AARG304
AHOH559
BLYS246
CGLU169
CARG304
CPO4407

site_idAC6
Number of Residues5
Detailsbinding site for residue EDO A 406
ChainResidue
ATHR49
AILE285
CHOH569
DTHR49
DILE285

site_idAC7
Number of Residues6
Detailsbinding site for residue PEG A 407
ChainResidue
AGLY132
AVAL133
AASN134
AHIS135
AGLN136
AGLN137

site_idAC8
Number of Residues2
Detailsbinding site for residue CL A 408
ChainResidue
AHIS-1
AHIS0

site_idAC9
Number of Residues21
Detailsbinding site for residue NAD B 401
ChainResidue
BGLY7
BGLY9
BARG10
BILE11
BASN32
BASP33
BLEU34
BSER95
BTHR96
BGLY97
BLEU98
BTHR119
BALA120
BCYS150
BALA181
BASN314
BTYR318
BHOH534
BHOH536
BHOH553
DHOH542

site_idAD1
Number of Residues5
Detailsbinding site for residue EDO B 402
ChainResidue
BASN165
BALA259
BHIS262
BALA263
BHOH540

site_idAD2
Number of Residues6
Detailsbinding site for residue EDO B 403
ChainResidue
BLEU163
BGLY167
BILE168
BGLU221
BLYS225
BSER248

site_idAD3
Number of Residues8
Detailsbinding site for residue EDO B 404
ChainResidue
BHOH504
CASP164
CASN165
CPHE166
BSER248
BSER249
BALA250
BARG304

site_idAD4
Number of Residues2
Detailsbinding site for residue EDO B 405
ChainResidue
BTYR253
BGLY298

site_idAD5
Number of Residues5
Detailsbinding site for residue EDO B 406
ChainResidue
AGLN296
BASP193
BARG195
BHOH503
BHOH561

site_idAD6
Number of Residues6
Detailsbinding site for residue PO4 B 407
ChainResidue
BSER149
BTHR151
BTHR209
BGLY210
BALA211
BHOH545

site_idAD7
Number of Residues5
Detailsbinding site for residue PEG B 408
ChainResidue
BVAL133
BASN134
BHIS135
BGLN136
BGLN137

site_idAD8
Number of Residues24
Detailsbinding site for residue NAD C 401
ChainResidue
CGLY7
CPHE8
CGLY9
CARG10
CILE11
CASN32
CASP33
CLEU34
CSER95
CTHR96
CGLY97
CLEU98
CTHR119
CALA120
CCYS150
CALA181
CASN314
CTYR318
CHOH506
CHOH526
CHOH542
CHOH549
CHOH557
CHOH561

site_idAD9
Number of Residues4
Detailsbinding site for residue EDO C 402
ChainResidue
AVAL35
CPRO189
CSER190
CARG191

site_idAE1
Number of Residues3
Detailsbinding site for residue EDO C 403
ChainResidue
CASP193
CTRP194
CHOH545

site_idAE2
Number of Residues5
Detailsbinding site for residue EDO C 404
ChainResidue
AARG304
AEDO403
CLYS246
CASP303
CARG304

site_idAE3
Number of Residues1
Detailsbinding site for residue EDO C 405
ChainResidue
CGLN296

site_idAE4
Number of Residues6
Detailsbinding site for residue PO4 C 406
ChainResidue
CSER149
CTHR151
CTHR209
CGLY210
CALA211
CHOH518

site_idAE5
Number of Residues7
Detailsbinding site for residue PO4 C 407
ChainResidue
AGLU169
AARG304
APO4405
CGLU170
CLYS246
CARG304
DLYS246

site_idAE6
Number of Residues1
Detailsbinding site for residue EDO C 408
ChainResidue
CALA300

site_idAE7
Number of Residues6
Detailsbinding site for residue PEG C 409
ChainResidue
CGLY132
CVAL133
CASN134
CHIS135
CGLN136
CGLN137

site_idAE8
Number of Residues21
Detailsbinding site for residue NAD D 401
ChainResidue
DGLY7
DPHE8
DGLY9
DARG10
DILE11
DASP33
DLEU34
DSER95
DTHR96
DGLY97
DLEU98
DTHR119
DALA120
DCYS150
DALA181
DASN314
DTYR318
DHOH510
DHOH533
DHOH543
DHOH583

site_idAE9
Number of Residues2
Detailsbinding site for residue EDO D 402
ChainResidue
DTHR128
DASN134

site_idAF1
Number of Residues8
Detailsbinding site for residue EDO D 403
ChainResidue
AASP164
AASN165
APHE166
DSER248
DSER249
DALA250
DARG304
DHOH560

site_idAF2
Number of Residues7
Detailsbinding site for residue PO4 D 404
ChainResidue
DSER149
DTHR151
DTHR209
DGLY210
DALA211
DHOH503
DHOH538

site_idAF3
Number of Residues5
Detailsbinding site for residue PEG D 405
ChainResidue
DVAL133
DASN134
DHIS135
DGLN136
DGLN137

Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
AALA148-LEU155

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P00362
ChainResidueDetails
ACYS150
BCYS150
CCYS150
DCYS150

site_idSWS_FT_FI2
Number of Residues36
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00362
ChainResidueDetails
AARG10
BARG10
BASP33
BLYS77
BTHR119
BSER149
BTHR180
BTHR209
BARG232
BASN314
CARG10
AASP33
CASP33
CLYS77
CTHR119
CSER149
CTHR180
CTHR209
CARG232
CASN314
DARG10
DASP33
ALYS77
DLYS77
DTHR119
DSER149
DTHR180
DTHR209
DARG232
DASN314
ATHR119
ASER149
ATHR180
ATHR209
AARG232
AASN314

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Activates thiol group during catalysis => ECO:0000250|UniProtKB:P00362
ChainResidueDetails
AHIS177
BHIS177
CHIS177
DHIS177

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon