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6IQV

Crystal Structure of Cell Surface Glyceraldehyde-3-Phosphate Dehydrogenase Complexed with Hg2+ from Lactobacillus plantarum

Functional Information from GO Data
ChainGOidnamespacecontents
A0006006biological_processglucose metabolic process
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
B0006006biological_processglucose metabolic process
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0050661molecular_functionNADP binding
B0051287molecular_functionNAD binding
C0006006biological_processglucose metabolic process
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0050661molecular_functionNADP binding
C0051287molecular_functionNAD binding
D0006006biological_processglucose metabolic process
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 Residues4
Detailsbinding site for residue EDO A 401
ChainResidue
AHIS47
AVAL62
AHOH505
DHOH506

site_idAC2
Number of Residues4
Detailsbinding site for residue HG A 402
ChainResidue
ACYS160
ALEU161
ATHR248
AALA318

site_idAC3
Number of Residues3
Detailsbinding site for residue HG A 403
ChainResidue
ATYR324
ACYS328
AARG20

site_idAC4
Number of Residues3
Detailsbinding site for residue HG A 404
ChainResidue
AILE13
ACYS101
ASER125

site_idAC5
Number of Residues7
Detailsbinding site for residue EDO A 405
ChainResidue
AARG15
ALEU16
AARG19
ALEU48
ALEU49
AASP52
AHOH568

site_idAC6
Number of Residues12
Detailsbinding site for residue TRS B 401
ChainResidue
AHOH552
AHOH556
BGLY208
BGLY241
BHOH557
BHOH559
BHOH587
CHOH555
DGLY208
DGLY241
DHOH526
DHOH561

site_idAC7
Number of Residues4
Detailsbinding site for residue EDO B 402
ChainResidue
BHIS47
BVAL62
BHOH530
CASP282

site_idAC8
Number of Residues3
Detailsbinding site for residue HG B 403
ChainResidue
BCYS160
BLEU161
BTHR248

site_idAC9
Number of Residues4
Detailsbinding site for residue HG B 404
ChainResidue
BARG20
BTYR324
BTHR327
BCYS328

site_idAD1
Number of Residues3
Detailsbinding site for residue HG B 405
ChainResidue
BGLY9
BGLY11
BCYS101

site_idAD2
Number of Residues5
Detailsbinding site for residue EDO C 401
ChainResidue
APHE201
BHOH514
CHIS47
CVAL62
CHOH502

site_idAD3
Number of Residues3
Detailsbinding site for residue HG C 402
ChainResidue
CARG20
CTYR324
CCYS328

site_idAD4
Number of Residues3
Detailsbinding site for residue HG C 403
ChainResidue
CCYS160
CLEU161
CTHR248

site_idAD5
Number of Residues6
Detailsbinding site for residue EDO D 401
ChainResidue
AASP282
AHOH620
DHIS47
DVAL62
DHOH524
DHOH540

site_idAD6
Number of Residues4
Detailsbinding site for residue HG D 402
ChainResidue
DLEU99
DGLU100
DCYS101
DMET330

site_idAD7
Number of Residues3
Detailsbinding site for residue HG D 403
ChainResidue
DCYS160
DLEU161
DTHR248

site_idAD8
Number of Residues4
Detailsbinding site for residue HG D 404
ChainResidue
DARG20
DTYR324
DTHR327
DCYS328

site_idAD9
Number of Residues5
Detailsbinding site for residue EDO D 405
ChainResidue
DARG15
DARG19
DLEU48
DTYR51
DASP52

246704

PDB entries from 2025-12-24

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