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6FZH

Crystal structure of a streptococcal dehydrogenase at 1.5 Angstroem resolution

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
Functional Information from PDB Data
site_idAC1
Number of Residues35
Detailsbinding site for residue NAD A 401
ChainResidue
AASN8
ATHR97
AGLY98
APHE99
APHE100
ATHR121
AALA122
ACYS152
APRO191
AASN316
ATYR320
AGLY9
AHOH516
AHOH596
AHOH597
AHOH598
AHOH628
AHOH643
AHOH661
AHOH677
AHOH703
AHOH704
AGLY11
AHOH708
AHOH709
AHOH714
AHOH716
AHOH739
AHOH742
AARG12
AILE13
AASP34
ALEU35
AARG78
AALA96

site_idAC2
Number of Residues7
Detailsbinding site for residue GOL A 402
ChainResidue
AASN39
AHIS43
ALYS46
ATYR47
AHOH523
AHOH705
BASP276

site_idAC3
Number of Residues34
Detailsbinding site for residue NAD B 401
ChainResidue
BGLY9
BGLY11
BARG12
BILE13
BASP34
BLEU35
BARG78
BALA96
BTHR97
BGLY98
BPHE99
BPHE100
BTHR121
BALA122
BPRO191
BASN316
BTYR320
BHOH596
BHOH601
BHOH606
BHOH623
BHOH627
BHOH630
BHOH645
BHOH654
BHOH673
BHOH680
BHOH682
BHOH721
BHOH725
BHOH733
BHOH759
BHOH760
BHOH896

site_idAC4
Number of Residues6
Detailsbinding site for residue PEG B 402
ChainResidue
BASN134
BHIS137
BASN268
BHOH514
BHOH542
BHOH863

site_idAC5
Number of Residues11
Detailsbinding site for residue GOL B 403
ChainResidue
BPRO123
BSER151
BTHR154
BGLY213
BALA214
BALA217
BHOH502
BHOH505
BHOH507
BHOH648
BHOH842

site_idAC6
Number of Residues5
Detailsbinding site for residue GOL B 404
ChainResidue
ATHR295
BARG198
BASN210
BHOH605
BHOH634

Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
AALA150-LEU157

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P00362
ChainResidueDetails
ACYS152
BCYS152

site_idSWS_FT_FI2
Number of Residues20
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00362
ChainResidueDetails
AARG78
ATHR121
ASER151
ATHR182
AARG199
ATHR212
AARG235
AASN316
BARG12
BASP34
BARG78
BTHR121
BSER151
BTHR182
BARG199
BTHR212
BARG235
BASN316
AARG12
AASP34

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Activates thiol group during catalysis => ECO:0000250|UniProtKB:Q6GIL8
ChainResidueDetails
AHIS179
BHIS179

219869

PDB entries from 2024-05-15

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