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5UR0

Crystallographic structure of glyceraldehyde-3-phosphate dehydrogenase from Naegleria gruberi

Functional Information from GO Data
ChainGOidnamespacecontents
A0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
A0005829cellular_componentcytosol
A0006006biological_processglucose metabolic process
A0006096biological_processglycolytic process
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
B0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
B0005829cellular_componentcytosol
B0006006biological_processglucose metabolic process
B0006096biological_processglycolytic process
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0050661molecular_functionNADP binding
B0051287molecular_functionNAD binding
C0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
C0005829cellular_componentcytosol
C0006006biological_processglucose metabolic process
C0006096biological_processglycolytic process
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0050661molecular_functionNADP binding
C0051287molecular_functionNAD binding
D0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
D0005829cellular_componentcytosol
D0006006biological_processglucose metabolic process
D0006096biological_processglycolytic process
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 Residues36
Detailsbinding site for residue NAD A 401
ChainResidue
AASN7
AMET36
AARG78
ASER96
ATHR97
AGLY98
ASER120
AALA121
ACSD149
AOCS149
AALA180
AGLY8
AASN314
ATYR318
AHOH519
AHOH521
AHOH523
AHOH530
AHOH551
AHOH552
AHOH558
AHOH602
AGLY10
AHOH603
AHOH642
AHOH675
AHOH677
AHOH691
AHOH698
CPRO188
AARG11
AILE12
AASN32
AASP33
AILE34
AMET35

site_idAC2
Number of Residues5
Detailsbinding site for residue PGE A 402
ChainResidue
ATHR125
APRO126
ATHR127
APHE128
ALEU216

site_idAC3
Number of Residues5
Detailsbinding site for residue NA A 403
ChainResidue
ASER20
AARG23
AVAL26
AHOH732
AHOH753

site_idAC4
Number of Residues36
Detailsbinding site for residue NAD B 401
ChainResidue
BASN7
BGLY8
BGLY10
BARG11
BILE12
BASN32
BASP33
BILE34
BMET35
BMET36
BARG78
BSER96
BTHR97
BGLY98
BILE99
BSER120
BALA121
BOCS149
BCSD149
BALA180
BASN314
BTYR318
BHOH519
BHOH523
BHOH531
BHOH561
BHOH584
BHOH611
BHOH624
BHOH626
BHOH628
BHOH629
BHOH640
BHOH644
BHOH673
DPRO188

site_idAC5
Number of Residues5
Detailsbinding site for residue NA B 402
ChainResidue
BSER20
BARG23
BVAL26
BHOH743
BHOH750

site_idAC6
Number of Residues37
Detailsbinding site for residue NAD C 401
ChainResidue
CSER96
CTHR97
CGLY98
CSER120
CALA121
COCS149
CCSD149
CALA180
CASN314
CTYR318
CHOH526
CHOH529
CHOH533
CHOH540
CHOH548
CHOH576
CHOH577
CHOH590
CHOH606
CHOH607
CHOH626
CHOH630
CHOH672
CHOH679
CHOH700
APRO188
CASN7
CGLY8
CGLY10
CARG11
CILE12
CASN32
CASP33
CILE34
CMET35
CMET36
CARG78

site_idAC7
Number of Residues6
Detailsbinding site for residue NA C 402
ChainResidue
CSER20
CARG23
CVAL26
CHOH724
CHOH727
CHOH743

site_idAC8
Number of Residues34
Detailsbinding site for residue NAD D 401
ChainResidue
DASN7
DGLY8
DGLY10
DARG11
DILE12
DASN32
DASP33
DILE34
DMET35
DMET36
DARG78
DSER96
DTHR97
DGLY98
DILE99
DSER120
DALA121
DOCS149
DCSD149
DALA180
DASN314
DTYR318
DHOH538
DHOH541
DHOH548
DHOH551
DHOH571
DHOH577
DHOH603
DHOH607
DHOH645
DHOH655
DHOH659
DHOH673

site_idAC9
Number of Residues6
Detailsbinding site for residue NA D 402
ChainResidue
DSER20
DARG23
DVAL26
DHOH699
DHOH738
DHOH769

Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
AALA147-LEU154

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PDB entries from 2026-03-25

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