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3ZCX

Structure of GAPDH from Thermosynechococcus elongatus

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
Functional Information from PDB Data
site_idAC1
Number of Residues27
DetailsBINDING SITE FOR RESIDUE NAD A 1000
ChainResidue
AGLY8
AALA99
ATHR100
AGLY101
ATHR123
AALA124
ACYS154
AASN317
ATYR321
AHOH2001
AHOH2002
APHE9
AHOH2035
AHOH2038
AHOH2062
AHOH2063
AHOH2117
AHOH2120
BHOH2057
BHOH2058
AGLY10
AARG11
AILE12
AASN35
AASP36
ATHR37
AARG81

site_idAC2
Number of Residues26
DetailsBINDING SITE FOR RESIDUE NAD B 1000
ChainResidue
AHOH2070
AHOH2072
BGLY8
BPHE9
BGLY10
BARG11
BILE12
BASN35
BASP36
BTHR37
BARG81
BALA99
BTHR100
BGLY101
BTHR123
BALA124
BCYS154
BASN317
BTYR321
BHOH2002
BHOH2003
BHOH2032
BHOH2051
BHOH2098
BHOH2101
BHOH2102

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

222415

PDB entries from 2024-07-10

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