Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6GG7

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
C0080153biological_processnegative regulation of reductive pentose-phosphate cycle
D0080153biological_processnegative regulation of reductive pentose-phosphate cycle
Functional Information from PDB Data
site_idAC1
Number of Residues34
Detailsbinding site for residue NAD B 1001
ChainResidue
AHOH1194
BARG81
BALA99
BTHR100
BGLY101
BPHE103
BTHR123
BALA124
BCYS154
BASN317
BTYR321
BGLY8
BHOH1135
BHOH1136
BHOH1160
BHOH1172
BHOH1180
BHOH1193
BHOH1202
BHOH1230
BHOH1234
CASP66
BPHE9
CARG71
CTYR73
CHOH105
CHOH110
DHOH110
BGLY10
BARG11
BILE12
BASN35
BASP36
BTHR37

site_idAC2
Number of Residues33
Detailsbinding site for residue NAD A 1001
ChainResidue
AGLY8
APHE9
AGLY10
AARG11
AILE12
AASN35
AASP36
ATHR37
AARG81
AALA99
ATHR100
AGLY101
APHE103
ATHR123
AALA124
ACYS154
AASN317
ATYR321
AHOH1139
AHOH1140
AHOH1147
AHOH1159
AHOH1181
AHOH1206
AHOH1221
AHOH1229
AHOH1230
AHOH1235
CHOH109
DASP66
DTYR73
DHOH108
DHOH113

Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
BALA152-LEU159

227344

PDB entries from 2024-11-13

PDB statisticsPDBj update infoContact PDBjnumon