Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4QX6

CRYSTAL STRUCTURE OF GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM STREPTOCOCCUS AGALACTIAE NEM316 at 2.46 ANGSTROM RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
A0005737cellular_componentcytoplasm
A0006006biological_processglucose metabolic 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
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
C0000166molecular_functionnucleotide binding
C0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
C0005737cellular_componentcytoplasm
C0006006biological_processglucose metabolic process
C0016491molecular_functionoxidoreductase activity
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0050661molecular_functionNADP binding
C0051287molecular_functionNAD binding
D0000166molecular_functionnucleotide binding
D0004365molecular_functionglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
D0005737cellular_componentcytoplasm
D0006006biological_processglucose metabolic process
D0016491molecular_functionoxidoreductase activity
D0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D0050661molecular_functionNADP binding
D0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE NAD A 401
ChainResidue
AGLY9
ATHR97
AGLY98
ATHR121
AALA122
ACYS152
AASN316
AHOH510
AHOH516
AHOH517
AHOH532
AGLY11
BPRO191
AARG12
AILE13
AASP34
ALEU35
AGLU77
AARG78
AALA96

site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NAD B 401
ChainResidue
APRO191
AHOH504
BGLY9
BGLY11
BARG12
BILE13
BASN33
BASP34
BLEU35
BGLU77
BARG78
BALA96
BTHR97
BGLY98
BPHE99
BPHE100
BTHR121
BALA122
BCYS152
BASN316
BTYR320
BHOH503
BHOH510
BHOH523

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE NAD C 401
ChainResidue
CASN8
CGLY9
CGLY11
CARG12
CILE13
CASN33
CASP34
CLEU35
CGLU77
CARG78
CALA96
CTHR97
CGLY98
CPHE99
CPHE100
CTHR121
CALA122
CCYS152
CTHR182
CASN316
CTYR320
CEDO402
CHOH508
DPRO191

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO C 402
ChainResidue
CGLU95
CTHR97
CGLY98
CPHE99
CPHE100
CALA101
CTHR121
CALA122
CNAD401

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO C 403
ChainResidue
CGLN185
CMET186
CILE187
DMET186
DILE187

site_idAC6
Number of Residues22
DetailsBINDING SITE FOR RESIDUE NAD D 401
ChainResidue
DCYS152
DASN316
DTYR320
DHOH506
DHOH519
CPRO191
CHOH503
DGLY9
DGLY11
DARG12
DILE13
DASN33
DASP34
DLEU35
DGLU77
DARG78
DALA96
DTHR97
DGLY98
DPHE100
DTHR121
DALA122

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

224201

PDB entries from 2024-08-28

PDB statisticsPDBj update infoContact PDBjnumon