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2EP7

Structural study of Project ID aq_1065 from Aquifex aeolicus VF5

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 Residues29
DetailsBINDING SITE FOR RESIDUE NAD A 401
ChainResidue
AGLY9
AALA96
ATHR97
AGLY98
APHE100
ATHR120
AALA121
ACYS152
ATHR182
AASN183
ALEU190
AGLY11
AASN322
AHOH410
AHOH419
AHOH425
AHOH428
AHOH434
AHOH450
AHOH524
AHOH526
AHOH527
AARG12
AILE13
AASN33
AASP34
ALEU35
AGLN77
ALYS78

site_idAC2
Number of Residues29
DetailsBINDING SITE FOR RESIDUE NAD B 402
ChainResidue
BGLY9
BGLY11
BARG12
BILE13
BASN33
BASP34
BLEU35
BGLN77
BLYS78
BALA96
BTHR97
BGLY98
BPHE100
BTHR120
BCYS152
BTHR182
BASN183
BLEU190
BPRO191
BASN322
BHOH403
BHOH406
BHOH415
BHOH426
BHOH431
BHOH432
BHOH454
BHOH513
BHOH514

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

site_idPS00430
Number of Residues70
DetailsTONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. maikvgingfgrigrsffraswgreeieivaindltdakhlahllkydsvhgifkgsveakd.....................................................DSIVVDGK
ChainResidueDetails
AMET1-LYS70

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 Residues10
DetailsBINDING: BINDING => ECO:0000269|Ref.2
ChainResidueDetails
AARG12
BASN322
AASP34
ALYS78
ATHR120
AASN322
BARG12
BASP34
BLYS78
BTHR120

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00362
ChainResidueDetails
ASER151
BARG197
BTHR210
BARG233
ATHR182
AASN183
AARG197
ATHR210
AARG233
BSER151
BTHR182
BASN183

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Activates thiol group during catalysis => ECO:0000250|UniProtKB:P00362
ChainResidueDetails
AHIS179
BHIS179

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
AHIS179
ACYS152

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1szj
ChainResidueDetails
BHIS179
BCYS152

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PDB entries from 2024-07-24

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