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6GHL

cyanobacterial GAPDH with full-length CP12

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0006006biological_processglucose metabolic process
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0046872molecular_functionmetal ion binding
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
B0000166molecular_functionnucleotide binding
B0006006biological_processglucose metabolic process
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0046872molecular_functionmetal ion binding
B0050661molecular_functionNADP binding
B0051287molecular_functionNAD binding
C0000166molecular_functionnucleotide binding
C0006006biological_processglucose metabolic process
C0016491molecular_functionoxidoreductase activity
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0046872molecular_functionmetal ion binding
C0050661molecular_functionNADP binding
C0051287molecular_functionNAD binding
D0000166molecular_functionnucleotide binding
D0006006biological_processglucose metabolic process
D0016491molecular_functionoxidoreductase activity
D0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D0046872molecular_functionmetal ion binding
D0050661molecular_functionNADP binding
D0051287molecular_functionNAD binding
E0080153biological_processnegative regulation of reductive pentose-phosphate cycle
F0080153biological_processnegative regulation of reductive pentose-phosphate cycle
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue NAD A 1001
ChainResidue
AGLY8
ATHR100
AGLY101
ATHR123
AALA124
ACYS154
AASN317
ATYR321
AHOH1107
AHOH1117
AHOH1119
APHE9
AHOH1129
DHOH1117
EGLU69
FHIS45
AGLY10
AARG11
AILE12
AASP36
ATHR37
AARG81
AALA99

site_idAC2
Number of Residues26
Detailsbinding site for residue NAD B 1001
ChainResidue
BGLY8
BPHE9
BGLY10
BARG11
BILE12
BASN35
BASP36
BTHR37
BASP80
BARG81
BALA99
BTHR100
BGLY101
BTHR123
BALA124
BCYS154
BTHR184
BASN317
BGLU318
BTYR321
BHOH1112
BHOH1118
BHOH1120
CHOH1110
FASP66
FTYR73

site_idAC3
Number of Residues20
Detailsbinding site for residue NAD C 1001
ChainResidue
CGLY8
CPHE9
CGLY10
CARG11
CILE12
CASN35
CASP36
CTHR37
CARG81
CALA99
CTHR100
CGLY101
CTHR123
CALA124
CCYS154
CASN317
CTYR321
CHOH1129
CHOH1130
CHOH1138

site_idAC4
Number of Residues8
Detailsbinding site for residue MLI C 1002
ChainResidue
CSER153
CCYS154
CTHR155
CARG199
CTHR212
CGLY213
CARG235
CHOH1141

site_idAC5
Number of Residues23
Detailsbinding site for residue NAD D 1001
ChainResidue
ETYR73
DGLY8
DPHE9
DGLY10
DARG11
DILE12
DASN35
DASP36
DTHR37
DARG81
DALA99
DGLY101
DTHR123
DALA124
DCYS154
DTHR184
DASN317
DTYR321
DHOH1102
DHOH1106
DHOH1110
DHOH1111
EASP66

Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
AALA152-LEU159

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PDB entries from 2024-07-10

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