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5HSS

Linalool dehydratase/isomerase: Ldi with monoterpene substrate

Functional Information from GO Data
ChainGOidnamespacecontents
A0016098biological_processmonoterpenoid metabolic process
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
A0016853molecular_functionisomerase activity
A0042597cellular_componentperiplasmic space
A0043694biological_processmonoterpene catabolic process
A0050486molecular_functionintramolecular hydroxytransferase activity
B0016098biological_processmonoterpenoid metabolic process
B0016829molecular_functionlyase activity
B0016836molecular_functionhydro-lyase activity
B0016853molecular_functionisomerase activity
B0042597cellular_componentperiplasmic space
B0043694biological_processmonoterpene catabolic process
B0050486molecular_functionintramolecular hydroxytransferase activity
C0016098biological_processmonoterpenoid metabolic process
C0016829molecular_functionlyase activity
C0016836molecular_functionhydro-lyase activity
C0016853molecular_functionisomerase activity
C0042597cellular_componentperiplasmic space
C0043694biological_processmonoterpene catabolic process
C0050486molecular_functionintramolecular hydroxytransferase activity
D0016098biological_processmonoterpenoid metabolic process
D0016829molecular_functionlyase activity
D0016836molecular_functionhydro-lyase activity
D0016853molecular_functionisomerase activity
D0042597cellular_componentperiplasmic space
D0043694biological_processmonoterpene catabolic process
D0050486molecular_functionintramolecular hydroxytransferase activity
E0016098biological_processmonoterpenoid metabolic process
E0016829molecular_functionlyase activity
E0016836molecular_functionhydro-lyase activity
E0016853molecular_functionisomerase activity
E0042597cellular_componentperiplasmic space
E0043694biological_processmonoterpene catabolic process
E0050486molecular_functionintramolecular hydroxytransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue PG0 A 401
ChainResidue
ALEU340
BILE40

site_idAC2
Number of Residues10
Detailsbinding site for residue 64Z A 402
ChainResidue
BASP38
BPHE39
BTYR44
AMET124
ACYS170
APHE176
ACYS179
ATYR239
ALEU294
ALEU341

site_idAC3
Number of Residues2
Detailsbinding site for residue PG0 B 401
ChainResidue
BLEU340
EPHE39

site_idAC4
Number of Residues6
Detailsbinding site for residue 650 B 402
ChainResidue
BTYR65
BPHE176
BCYS179
BLEU294
EPHE39
ETYR44

site_idAC5
Number of Residues9
Detailsbinding site for residue 650 C 401
ChainResidue
CTYR65
CMET124
CCYS170
CPHE176
CCYS179
CTYR239
CLEU294
DPHE39
DTYR44

site_idAC6
Number of Residues1
Detailsbinding site for residue PG0 D 401
ChainResidue
DPHE39

site_idAC7
Number of Residues2
Detailsbinding site for residue PG0 D 402
ChainResidue
APHE39
DLEU340

site_idAC8
Number of Residues10
Detailsbinding site for residue 64Z D 403
ChainResidue
AASP38
APHE39
ATYR44
DMET124
DCYS170
DPHE176
DCYS179
DTYR239
DLEU294
DLEU341

site_idAC9
Number of Residues1
Detailsbinding site for residue PG0 E 401
ChainResidue
EPRO59

site_idAD1
Number of Residues10
Detailsbinding site for residue 64Z E 402
ChainResidue
CASP38
CPHE39
CTYR44
ETYR65
EMET124
ECYS170
EPHE176
ECYS179
ETYR239
ELEU341

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|DOI:10.1021/acscatal.0c02958
ChainResidueDetails
AASP38
BASP38
CASP38
DASP38
EASP38

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:27062179, ECO:0007744|PDB:5HSS
ChainResidueDetails
ACYS170
BCYS170
CCYS170
DCYS170
ECYS170

227344

PDB entries from 2024-11-13

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