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3B1K

Crystal structure of Glyceraldehyde-3-Phosphate Dehydrogenase complexed with CP12 in the absence of copper from Synechococcus 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
A0043891molecular_functionglyceraldehyde-3-phosphate dehydrogenase [NAD(P)+] (phosphorylating) activity
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
B0043891molecular_functionglyceraldehyde-3-phosphate dehydrogenase [NAD(P)+] (phosphorylating) activity
B0046872molecular_functionmetal ion binding
B0050661molecular_functionNADP binding
B0051287molecular_functionNAD binding
G0000166molecular_functionnucleotide binding
G0006006biological_processglucose metabolic process
G0016491molecular_functionoxidoreductase activity
G0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
G0043891molecular_functionglyceraldehyde-3-phosphate dehydrogenase [NAD(P)+] (phosphorylating) activity
G0046872molecular_functionmetal ion binding
G0050661molecular_functionNADP binding
G0051287molecular_functionNAD binding
H0000166molecular_functionnucleotide binding
H0006006biological_processglucose metabolic process
H0016491molecular_functionoxidoreductase activity
H0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
H0043891molecular_functionglyceraldehyde-3-phosphate dehydrogenase [NAD(P)+] (phosphorylating) activity
H0046872molecular_functionmetal ion binding
H0050661molecular_functionNADP binding
H0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE NAD A 340
ChainResidue
AGLY11
AGLY100
AVAL101
APHE102
ATHR122
AALA123
ACYS155
ALEU186
AASN318
AGLU319
CTYR73
AARG12
HSER194
JGLU69
AILE13
AASN35
AASN36
ATHR37
AARG80
ASER98
ATHR99

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE NAD B 340
ChainResidue
BGLY9
BPHE10
BGLY11
BARG12
BILE13
BASN35
BASN36
BTHR37
BASP79
BARG80
BSER98
BTHR99
BGLY100
BTHR122
BCYS155
BLEU186
BASN318
DASP66
DTYR73
DASP75
IGLU69

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE NAD G 340
ChainResidue
BSER194
GASN8
GGLY9
GPHE10
GGLY11
GARG12
GILE13
GASN35
GASN36
GTHR37
GASP79
GSER98
GTHR99
GGLY100
GPHE102
GTHR122
GALA123
GCYS155
GLEU186
GASN318
GGLU319
ITYR73

site_idAC4
Number of Residues19
DetailsBINDING SITE FOR RESIDUE NAD H 340
ChainResidue
HGLY9
HGLY11
HARG12
HILE13
HASN35
HASN36
HTHR37
HARG80
HSER98
HTHR99
HGLY100
HTHR122
HALA123
HCYS155
HLEU186
HASN318
HGLU319
HTYR322
JTYR73

Functional Information from PROSITE/UniProt
site_idPS00071
Number of Residues8
DetailsGAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL
ChainResidueDetails
AALA153-LEU160

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PDB entries from 2025-10-29

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