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1W57

Structure of the Bifunctional IspDF from Campylobacter jejuni containing Zn

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0008299biological_processisoprenoid biosynthetic process
A0008685molecular_function2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity
A0016114biological_processterpenoid biosynthetic process
A0016740molecular_functiontransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0016829molecular_functionlyase activity
A0019288biological_processisopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway
A0046872molecular_functionmetal ion binding
A0050518molecular_function2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity
A0070567molecular_functioncytidylyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A1371
ChainResidue
AASP217
AHIS219
AHIS243
AHIS251
AHOH2057

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE C5P A1372
ChainResidue
AGLU268
AALA309
APRO312
ALYS313
ALEU314
ALYS315
ALYS318
AALA340
ATHR341
ATHR342
AGLU344
AHOH2041
AHOH2055
AHOH2057
AASP217
AASP265
AILE266
AGLY267

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE C5P A1373
ChainResidue
ALEU9
AALA10
AALA11
ATHR53
AGLY73
AASP74
ATHR75
AARG76
ASER79
AASP96
AVAL97
AALA98
AARG139
ALYS191

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GPP A1374
ChainResidue
APHE216
AMET308
AGLY347
APHE348
AARG351

Functional Information from PROSITE/UniProt
site_idPS01295
Number of Residues8
DetailsISPD 4-diphosphocytidyl-2C-methyl-D-erythritol synthase signature. VMVSDVAR
ChainResidueDetails
AVAL92-ARG99

site_idPS01350
Number of Residues16
DetailsISPF 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase signature. SDGDVLaHSltDAilG
ChainResidueDetails
ASER244-GLY259

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues17
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P62617","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_01520","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P62617","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_01520","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Positions MEP for the nucleophilic attack","evidences":[{"source":"HAMAP-Rule","id":"MF_01520","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P62617","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_01520","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hv9
ChainResidueDetails
AARG16

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PDB entries from 2025-07-16

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