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5L12

Crystal structure of 2C-methyl-D-erythritol 2,4-clycodiphosphate synthase from BURKHOLDERIA PSEUDOMALLEI double mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0008685molecular_function2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity
A0016114biological_processterpenoid biosynthetic process
A0019288biological_processisopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway
B0008685molecular_function2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity
B0016114biological_processterpenoid biosynthetic process
B0019288biological_processisopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway
C0008685molecular_function2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity
C0016114biological_processterpenoid biosynthetic process
C0019288biological_processisopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 201
ChainResidue
AASP10
AHIS12
AHIS44
AHOH408

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN B 201
ChainResidue
BASP10
BHIS12
BHIS44
BHOH353

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN C 201
ChainResidue
CHIS12
CHIS44
CHOH383
CASP10

Functional Information from PROSITE/UniProt
site_idPS01350
Number of Residues16
DetailsISPF 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase signature. SDADVLlHAitDAlfG
ChainResidueDetails
ASER37-GLY52

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues30
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00107","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues5
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_00107","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

253795

PDB entries from 2026-05-20

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