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5I3T

Native Structure of the Linalool Dehydratase-Isomerase from Castellaniella defragrans

Functional Information from PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue BU2 A 501
ChainResidue
ATYR269

site_idAC2
Number of Residues1
Detailsbinding site for residue K A 503
ChainResidue
ACYS209

site_idAC3
Number of Residues1
Detailsbinding site for residue CL B 501
ChainResidue
BHOH703

site_idAC4
Number of Residues1
Detailsbinding site for residue K B 502
ChainResidue
BCYS209

site_idAC5
Number of Residues1
Detailsbinding site for residue CL C 501
ChainResidue
CHOH694

site_idAC6
Number of Residues4
Detailsbinding site for residue BU2 D 501
ChainResidue
DTYR95
DTYR269
DTRP273
DLEU371

site_idAC7
Number of Residues1
Detailsbinding site for residue CL D 502
ChainResidue
DHOH695

site_idAC8
Number of Residues5
Detailsbinding site for residue CL D 503
ChainResidue
DARG37
DLEU38
DALA39
DTYR44
DGLU350

site_idAC9
Number of Residues1
Detailsbinding site for residue K D 504
ChainResidue
DCYS209

site_idAD1
Number of Residues3
Detailsbinding site for residue BU2 E 501
ChainResidue
BLEU370
EASP68
EPHE69

site_idAD2
Number of Residues1
Detailsbinding site for residue CL E 502
ChainResidue
EHOH695

site_idAD3
Number of Residues1
Detailsbinding site for residue K E 503
ChainResidue
ECYS209

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
AASP68
BASP68
CASP68
DASP68
EASP68

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:27062179, ECO:0007744|PDB:5HSS
ChainResidueDetails
ACYS200
BCYS200
CCYS200
DCYS200
ECYS200

222415

PDB entries from 2024-07-10

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