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6X2E

Crystal Structure of Chlamydia trachomatis mixed (apo/holo) Glyceraldehyde 3-phosphate dehydrogenase

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 Residues29
Detailsbinding site for residue NAD A 400
ChainResidue
AGLY7
AGLY97
ALEU98
ATHR119
AALA120
ACYS150
AALA181
AASN314
ATYR318
AHOH529
AHOH531
APHE8
AHOH534
AHOH549
AHOH553
AHOH556
AHOH578
AHOH585
AHOH592
AHOH628
AHOH659
CHOH546
AGLY9
AARG10
AILE11
AASP33
ALEU34
ASER95
ATHR96

site_idAC2
Number of Residues32
Detailsbinding site for residue NAD C 400
ChainResidue
CGLY7
CPHE8
CGLY9
CARG10
CILE11
CASN32
CASP33
CLEU34
CLYS77
CSER95
CTHR96
CGLY97
CLEU98
CTHR119
CALA120
CALA181
CASN314
CTYR318
CHOH507
CHOH526
CHOH537
CHOH552
CHOH568
CHOH575
CHOH578
CHOH579
CHOH583
CHOH589
CHOH597
CHOH599
CHOH637
CHOH643

site_idAC3
Number of Residues23
Detailsbinding site for residue NAD D 400
ChainResidue
DGLY7
DPHE8
DGLY9
DARG10
DILE11
DASP33
DLEU34
DSER95
DTHR96
DGLY97
DLEU98
DTHR119
DALA120
DCYS150
DALA181
DASN314
DTYR318
DHOH527
DHOH543
DHOH547
DHOH556
DHOH568
DHOH624

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

223532

PDB entries from 2024-08-07

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