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5O3Z

Crystal structure of Sorbitol-6-Phosphate 2-dehydrogenase SrlD from Erwinia amylovora

Functional Information from GO Data
ChainGOidnamespacecontents
A0009010molecular_functionsorbitol-6-phosphate 2-dehydrogenase activity
A0016491molecular_functionoxidoreductase activity
B0009010molecular_functionsorbitol-6-phosphate 2-dehydrogenase activity
B0016491molecular_functionoxidoreductase activity
C0009010molecular_functionsorbitol-6-phosphate 2-dehydrogenase activity
C0016491molecular_functionoxidoreductase activity
D0009010molecular_functionsorbitol-6-phosphate 2-dehydrogenase activity
D0016491molecular_functionoxidoreductase activity
E0009010molecular_functionsorbitol-6-phosphate 2-dehydrogenase activity
E0016491molecular_functionoxidoreductase activity
F0009010molecular_functionsorbitol-6-phosphate 2-dehydrogenase activity
F0016491molecular_functionoxidoreductase activity
G0009010molecular_functionsorbitol-6-phosphate 2-dehydrogenase activity
G0016491molecular_functionoxidoreductase activity
H0009010molecular_functionsorbitol-6-phosphate 2-dehydrogenase activity
H0016491molecular_functionoxidoreductase activity
I0009010molecular_functionsorbitol-6-phosphate 2-dehydrogenase activity
I0016491molecular_functionoxidoreductase activity
J0009010molecular_functionsorbitol-6-phosphate 2-dehydrogenase activity
J0016491molecular_functionoxidoreductase activity
K0009010molecular_functionsorbitol-6-phosphate 2-dehydrogenase activity
K0016491molecular_functionoxidoreductase activity
L0009010molecular_functionsorbitol-6-phosphate 2-dehydrogenase activity
L0016491molecular_functionoxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CL A 301
ChainResidue
ATHR253
AGLY254
AGLY255
BTHR246
BGLN248

site_idAC2
Number of Residues5
Detailsbinding site for residue CL B 301
ChainResidue
BGLY255
ATHR246
AGLN248
BTHR253
BGLY254

site_idAC3
Number of Residues5
Detailsbinding site for residue CL C 301
ChainResidue
CTHR253
CGLY254
CGLY255
DTYR244
DGLN248

site_idAC4
Number of Residues5
Detailsbinding site for residue CL D 301
ChainResidue
CTHR246
CGLN248
DTHR253
DGLY254
DGLY255

site_idAC5
Number of Residues5
Detailsbinding site for residue CL E 301
ChainResidue
ETHR253
EGLY254
EGLY255
FTHR246
FGLN248

site_idAC6
Number of Residues6
Detailsbinding site for residue CL F 301
ChainResidue
ECYS245
ETHR246
EGLN248
FTHR253
FGLY254
FGLY255

site_idAC7
Number of Residues6
Detailsbinding site for residue CL G 301
ChainResidue
GTHR253
GGLY254
GGLY255
HCYS245
HTHR246
HGLN248

site_idAC8
Number of Residues6
Detailsbinding site for residue CL H 301
ChainResidue
GCYS245
GTHR246
GGLN248
HTHR253
HGLY254
HGLY255

site_idAC9
Number of Residues5
Detailsbinding site for residue CL I 301
ChainResidue
ITHR253
IGLY254
IGLY255
JCYS245
JGLN248

site_idAD1
Number of Residues6
Detailsbinding site for residue CL J 301
ChainResidue
ICYS245
ITHR246
IGLN248
JTHR253
JGLY254
JGLY255

site_idAD2
Number of Residues6
Detailsbinding site for residue CL K 301
ChainResidue
KTHR253
KGLY254
KGLY255
LTYR244
LTHR246
LGLN248

site_idAD3
Number of Residues5
Detailsbinding site for residue CL L 301
ChainResidue
KTHR246
KGLN248
LTHR253
LGLY254
LGLY255

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SksgkvgskhNsgYSAAKFGGvGLTqSLA
ChainResidueDetails
ASER141-ALA169

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PDB entries from 2026-03-11

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