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3DON

Crystal structure of shikimate dehydrogenase from Staphylococcus epidermidis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004764molecular_functionshikimate 3-dehydrogenase (NADP+) activity
A0008652biological_processamino acid biosynthetic process
A0009073biological_processaromatic amino acid family biosynthetic process
A0009423biological_processchorismate biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0019632biological_processshikimate metabolic process
A0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 278
ChainResidue
AGLN77
AVAL81
AGLY131
AASN134
AGLU135
ALYS138
AHOH312
AHOH465

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00222
ChainResidueDetails
ALYS64

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000269|PubMed:19215302
ChainResidueDetails
ASER13
ATHR60
AASN85
AASP100
AGLN239

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00222
ChainResidueDetails
AGLU76
AGLY124
AASN148
AILE209
ATYR211
AGLY232

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Plays a major role in the catalytic process and a minor role in the substrate binding => ECO:0000269|PubMed:19215302
ChainResidueDetails
ATYR211

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1nvt
ChainResidueDetails
AASP91

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PDB entries from 2024-07-24

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