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4CVH

Crystal structure of human isoprenoid synthase domain-containing protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006486biological_processprotein glycosylation
A0007411biological_processaxon guidance
A0008299biological_processisoprenoid biosynthetic process
A0016740molecular_functiontransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0035269biological_processprotein O-linked mannosylation
A0042803molecular_functionprotein homodimerization activity
A0047349molecular_functionD-ribitol-5-phosphate cytidylyltransferase activity
A0070567molecular_functioncytidylyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1452
ChainResidue
ATHR125
AARG126
AHIS127
ALEU234
AGLU235
AGLY237

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 1453
ChainResidue
AHIS114
AGLU85
ATYR112
AGLN113

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1454
ChainResidue
AARG128
AASN132
AGLU293

Functional Information from PROSITE/UniProt
site_idPS01295
Number of Residues8
DetailsISPD 4-diphosphocytidyl-2C-methyl-D-erythritol synthase signature. VIIHDAVR
ChainResidueDetails
AVAL152-ARG159

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:Q46893
ChainResidueDetails
AARG59
ALYS66

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Positions substrate for the nucleophilic attack => ECO:0000250|UniProtKB:Q46893
ChainResidueDetails
AARG205
ALYS263

237423

PDB entries from 2025-06-11

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