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1DB3

E.COLI GDP-MANNOSE 4,6-DEHYDRATASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0008446molecular_functionGDP-mannose 4,6-dehydratase activity
A0009242biological_processcolanic acid biosynthetic process
A0016829molecular_functionlyase activity
A0019673biological_processGDP-mannose metabolic process
A0042351biological_process'de novo' GDP-L-fucose biosynthetic process
A0042803molecular_functionprotein homodimerization activity
A0070401molecular_functionNADP+ binding
Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. PqkettpfypRspYAVAKLYAyWITvNYR
ChainResidueDetails
APRO143-ARG171

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:10673432
ChainResidueDetails
ATHR132

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:10673432
ChainResidueDetails
AGLU134
ATYR156

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00955
ChainResidueDetails
AGLY8
AASP63
ALEU85
ATYR100
AHIS186
AARG191

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
ALYS160

Catalytic Information from CSA
site_idCSA1
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 20139699, 19459932, 17974560
ChainResidueDetails
AGLU134
ALYS160
ATHR132
ATYR156

site_idMCSA1
Number of Residues4
DetailsM-CSA 487
ChainResidueDetails
ATHR132proton shuttle (general acid/base)
AGLU134proton shuttle (general acid/base)
ATYR156electrostatic stabiliser, proton shuttle (general acid/base)
ALYS160electrostatic stabiliser, modifies pKa

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PDB entries from 2025-06-18

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