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7JWK

Crystal Structure of Glyceraldehyde-3-phosphate Dehydrogenase (GAPDH) from Mycoplasma genitalium 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
A0006735biological_processNADH regeneration
A0009986cellular_componentcell surface
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0044650biological_processadhesion of symbiont to host cell
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
A0140032molecular_functionglycosylation-dependent protein binding
B0000166molecular_functionnucleotide binding
B0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
B0005737cellular_componentcytoplasm
B0006006biological_processglucose metabolic process
B0006096biological_processglycolytic process
B0006735biological_processNADH regeneration
B0009986cellular_componentcell surface
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0044650biological_processadhesion of symbiont to host cell
B0050661molecular_functionNADP binding
B0051287molecular_functionNAD binding
B0140032molecular_functionglycosylation-dependent protein binding
C0000166molecular_functionnucleotide binding
C0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
C0005737cellular_componentcytoplasm
C0006006biological_processglucose metabolic process
C0006096biological_processglycolytic process
C0006735biological_processNADH regeneration
C0009986cellular_componentcell surface
C0016491molecular_functionoxidoreductase activity
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0044650biological_processadhesion of symbiont to host cell
C0050661molecular_functionNADP binding
C0051287molecular_functionNAD binding
C0140032molecular_functionglycosylation-dependent protein binding
D0000166molecular_functionnucleotide binding
D0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
D0005737cellular_componentcytoplasm
D0006006biological_processglucose metabolic process
D0006096biological_processglycolytic process
D0006735biological_processNADH regeneration
D0009986cellular_componentcell surface
D0016491molecular_functionoxidoreductase activity
D0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D0044650biological_processadhesion of symbiont to host cell
D0050661molecular_functionNADP binding
D0051287molecular_functionNAD binding
D0140032molecular_functionglycosylation-dependent protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues33
Detailsbinding site for residue NAD A 401
ChainResidue
AGLY14
ASER101
ATHR102
AGLY103
ASER125
AALA126
ACYS157
AALA188
AASN319
ATYR323
APO4403
AGLY16
AHOH510
AHOH512
AHOH513
AHOH526
AHOH533
AHOH552
AHOH559
AHOH565
AHOH568
AHOH575
AARG17
AHOH577
AHOH581
AHOH592
AHOH610
AILE18
AASN38
AASP39
ALEU40
AGLU82
ALYS83

site_idAC2
Number of Residues11
Detailsbinding site for residue PO4 A 402
ChainResidue
ASER156
ACYS157
ATHR158
AHIS184
ATHR215
AGLY216
APO4403
AHOH544
AHOH563
AHOH575
AHOH579

site_idAC3
Number of Residues9
Detailsbinding site for residue PO4 A 403
ChainResidue
ATHR187
AARG202
AARG238
ANAD401
APO4402
AHOH501
AHOH505
AHOH526
AHOH544

site_idAC4
Number of Residues5
Detailsbinding site for residue PEG A 404
ChainResidue
ALYS275
ACYS277
AASP285
ASER289
DTYR52

site_idAC5
Number of Residues31
Detailsbinding site for residue NAD B 401
ChainResidue
BGLY14
BGLY16
BARG17
BILE18
BASP39
BLEU40
BLYS83
BSER101
BTHR102
BGLY103
BARG104
BPHE105
BSER125
BALA126
BCYS157
BALA188
BASN319
BTYR323
BPO4403
BHOH508
BHOH522
BHOH543
BHOH548
BHOH549
BHOH552
BHOH557
BHOH564
BHOH587
BHOH588
BHOH604
DHOH520

site_idAC6
Number of Residues10
Detailsbinding site for residue PO4 B 402
ChainResidue
BSER156
BCYS157
BTHR158
BHIS184
BTHR215
BGLY216
BHOH529
BHOH537
BHOH551
BHOH587

site_idAC7
Number of Residues9
Detailsbinding site for residue PO4 B 403
ChainResidue
BTHR187
BASP189
BARG202
BARG238
BNAD401
BHOH502
BHOH513
BHOH529
BHOH545

site_idAC8
Number of Residues7
Detailsbinding site for residue PEG B 404
ChainResidue
BLYS275
BCYS277
BASP285
BSER289
BILE294
CTYR52
CGLU58

site_idAC9
Number of Residues33
Detailsbinding site for residue NAD C 401
ChainResidue
CGLY14
CGLY16
CARG17
CILE18
CASN38
CASP39
CLEU40
CGLU82
CLYS83
CSER101
CTHR102
CGLY103
CARG104
CPHE105
CSER125
CALA126
CCYS157
CALA188
CASN319
CTYR323
CPO4403
CHOH520
CHOH532
CHOH534
CHOH543
CHOH544
CHOH549
CHOH554
CHOH558
CHOH563
CHOH568
CHOH571
CHOH579

site_idAD1
Number of Residues10
Detailsbinding site for residue PO4 C 402
ChainResidue
CSER156
CCYS157
CTHR158
CHIS184
CTHR215
CGLY216
CHOH512
CHOH523
CHOH553
CHOH568

site_idAD2
Number of Residues9
Detailsbinding site for residue PO4 C 403
ChainResidue
CTHR187
CASP189
CARG202
CARG238
CNAD401
CHOH501
CHOH512
CHOH526
CHOH545

site_idAD3
Number of Residues4
Detailsbinding site for residue PEG C 404
ChainResidue
CLYS275
CCYS277
CASP285
CSER289

site_idAD4
Number of Residues26
Detailsbinding site for residue NAD D 401
ChainResidue
BHOH519
DGLY14
DGLY16
DARG17
DILE18
DASN38
DASP39
DLEU40
DLYS83
DSER101
DTHR102
DGLY103
DPHE105
DSER125
DALA126
DCYS157
DALA188
DASN319
DPO4403
DHOH503
DHOH508
DHOH514
DHOH527
DHOH528
DHOH529
DHOH558

site_idAD5
Number of Residues10
Detailsbinding site for residue PO4 D 402
ChainResidue
DSER156
DCYS157
DTHR158
DHIS184
DTHR215
DGLY216
DPO4403
DHOH506
DHOH508
DHOH509

site_idAD6
Number of Residues10
Detailsbinding site for residue PO4 D 403
ChainResidue
DTHR187
DASP189
DARG202
DARG238
DNAD401
DPO4402
DHOH501
DHOH506
DHOH508
DHOH556

site_idAD7
Number of Residues3
Detailsbinding site for residue PEG D 404
ChainResidue
DCYS277
DASP285
DSER289

Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
AALA155-LEU162

site_idPS00584
Number of Residues14
DetailsPFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. KTiSSDDkiiSAAS
ChainResidueDetails
ALYS143-SER156

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P00362
ChainResidueDetails
ACYS157
BCYS157
CCYS157
DCYS157

site_idSWS_FT_FI2
Number of Residues40
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00362
ChainResidueDetails
ASER156
ATHR187
AARG202
ATHR215
AARG238
AASN319
BARG17
BASP39
BLYS83
BSER125
BSER156
BTHR187
BARG202
BTHR215
BARG238
BASN319
CARG17
CASP39
CLYS83
CSER125
CSER156
CTHR187
CARG202
CTHR215
CARG238
CASN319
DARG17
DASP39
DLYS83
DSER125
DSER156
DTHR187
DARG202
DTHR215
DARG238
DASN319
AASP39
ALYS83
ASER125
AARG17

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Activates thiol group during catalysis => ECO:0000250|UniProtKB:P00362
ChainResidueDetails
DHIS184
AHIS184
BHIS184
CHIS184

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PDB entries from 2024-06-12

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