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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

4UXA

Improved variant of (R)-selective manganese-dependent hydroxynitrile lyase from bacteria

Functional Information from GO Data
ChainGOidnamespacecontents
A0016829molecular_functionlyase activity
A0046593molecular_functionmandelonitrile lyase activity
A0046872molecular_functionmetal ion binding
B0016829molecular_functionlyase activity
B0046593molecular_functionmandelonitrile lyase activity
B0046872molecular_functionmetal ion binding
C0016829molecular_functionlyase activity
C0046593molecular_functionmandelonitrile lyase activity
C0046872molecular_functionmetal ion binding
D0016829molecular_functionlyase activity
D0046593molecular_functionmandelonitrile lyase activity
D0046872molecular_functionmetal ion binding
E0016829molecular_functionlyase activity
E0046593molecular_functionmandelonitrile lyase activity
E0046872molecular_functionmetal ion binding
F0016829molecular_functionlyase activity
F0046593molecular_functionmandelonitrile lyase activity
F0046872molecular_functionmetal ion binding
G0016829molecular_functionlyase activity
G0046593molecular_functionmandelonitrile lyase activity
G0046872molecular_functionmetal ion binding
H0016829molecular_functionlyase activity
H0046593molecular_functionmandelonitrile lyase activity
H0046872molecular_functionmetal ion binding
I0016829molecular_functionlyase activity
I0046593molecular_functionmandelonitrile lyase activity
I0046872molecular_functionmetal ion binding
J0016829molecular_functionlyase activity
J0046593molecular_functionmandelonitrile lyase activity
J0046872molecular_functionmetal ion binding
K0016829molecular_functionlyase activity
K0046593molecular_functionmandelonitrile lyase activity
K0046872molecular_functionmetal ion binding
L0016829molecular_functionlyase activity
L0046593molecular_functionmandelonitrile lyase activity
L0046872molecular_functionmetal ion binding
M0016829molecular_functionlyase activity
M0046593molecular_functionmandelonitrile lyase activity
M0046872molecular_functionmetal ion binding
N0016829molecular_functionlyase activity
N0046593molecular_functionmandelonitrile lyase activity
N0046872molecular_functionmetal ion binding
O0016829molecular_functionlyase activity
O0046593molecular_functionmandelonitrile lyase activity
O0046872molecular_functionmetal ion binding
P0016829molecular_functionlyase activity
P0046593molecular_functionmandelonitrile lyase activity
P0046872molecular_functionmetal ion binding
Q0016829molecular_functionlyase activity
Q0046593molecular_functionmandelonitrile lyase activity
Q0046872molecular_functionmetal ion binding
R0016829molecular_functionlyase activity
R0046593molecular_functionmandelonitrile lyase activity
R0046872molecular_functionmetal ion binding
S0016829molecular_functionlyase activity
S0046593molecular_functionmandelonitrile lyase activity
S0046872molecular_functionmetal ion binding
T0016829molecular_functionlyase activity
T0046593molecular_functionmandelonitrile lyase activity
T0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 200
ChainResidue
AHIS53
AHIS55
AGLN59
AHIS94
AHIS96
AHOH2045
site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 200
ChainResidue
BHIS94
BHIS96
BHOH2055
BHIS53
BHIS55
BGLN59
site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN C 200
ChainResidue
CHIS53
CHIS55
CGLN59
CHIS94
CHIS96
CHOH2051
site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN D 200
ChainResidue
DHIS53
DHIS55
DGLN59
DHIS94
DHIS96
DHOH2064
site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN E 200
ChainResidue
EHIS53
EHIS55
EGLN59
EHIS94
EHIS96
EHOH2039
site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN F 200
ChainResidue
FHIS53
FHIS55
FGLN59
FHIS94
FHIS96
FHOH2048
site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN G 200
ChainResidue
GHIS53
GHIS55
GGLN59
GHIS94
GHIS96
GHOH2041
site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN H 200
ChainResidue
HHIS53
HHIS55
HGLN59
HHIS94
HHIS96
HHOH2044
site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN I 200
ChainResidue
IHIS53
IHIS55
IGLN59
IHIS94
IHIS96
IHOH2044
site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN J 200
ChainResidue
JHIS53
JHIS55
JGLN59
JHIS94
JHIS96
JHOH2036
site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN K 200
ChainResidue
KHIS53
KHIS55
KGLN59
KHIS94
KHIS96
KHOH2055
site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN L 200
ChainResidue
LHIS53
LHIS55
LGLN59
LHIS94
LHIS96
LHOH2045
site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN M 200
ChainResidue
MHIS53
MHIS55
MGLN59
MHIS94
MHIS96
MHOH2043
site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN N 200
ChainResidue
NHIS53
NHIS55
NGLN59
NHIS94
NHIS96
NHOH2046
site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN O 200
ChainResidue
OHIS53
OHIS55
OGLN59
OHIS94
OHIS96
OHOH2042
site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN P 200
ChainResidue
PHIS53
PHIS55
PGLN59
PHIS94
PHIS96
PHOH2045
site_idBC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN Q 200
ChainResidue
QHIS94
QHIS96
QHOH2035
QHIS53
QHIS55
QGLN59
site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN R 200
ChainResidue
RHIS53
RHIS55
RGLN59
RHIS94
RHIS96
RHOH2040
site_idCC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN S 200
ChainResidue
SHIS53
SHIS55
SGLN59
SHIS94
SHIS96
SHOH2026
site_idCC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN T 200
ChainResidue
THIS53
THIS55
TGLN59
THIS94
THIS96
THOH2030
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1240
DetailsDomain: {"description":"Cupin type-2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues100
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23981508","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2015","firstPage":"0","lastPage":"0","volume":"0","journal":"ChemCatChem","title":"Improving the Properties of Bacterial R-Selective Hydroxynitrile Lyases for Industrial Applications.","authors":["Wiedner R.","Kothbauer B.","Pavkov-Keller T.","Gruber-Khadjawi M.","Grube K.","Schwab H.","Steiner K."],"citationCrossReferences":[{"database":"DOI","id":"10.1002/CCTC.201402742"}]}},{"source":"PDB","id":"4BIF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UXA","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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