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4R9K

Structure of thermostable eightfold mutant of limonene epoxide hydrolase from Rhodococcus erythropolis

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0018744molecular_functionlimonene-1,2-epoxide hydrolase activity
B0016787molecular_functionhydrolase activity
B0018744molecular_functionlimonene-1,2-epoxide hydrolase activity
C0016787molecular_functionhydrolase activity
C0018744molecular_functionlimonene-1,2-epoxide hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 201
ChainResidue
ASER12
ALYS13
AASP50
AGOL202
AHOH342
BLYS13
BTHR128
BHOH301
BHOH394

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 202
ChainResidue
ALYS13
ATHR128
AGOL201
AHOH303
BSER12
BLYS13
BASP50
BHOH301
BHOH394

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE HYH A 203
ChainResidue
AARG99
AASP101
AASP132
APHE134
APHE139
AHOH364

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 201
ChainResidue
BGLU49
BARG64
BASP65
BHOH312

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE HYH B 202
ChainResidue
BARG99
BASP101
BLEU103
BASP132
BPHE139
BHOH303

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL C 201
ChainResidue
CSER12
CLYS13
CLYS13
CASP50
CTHR128
CHOH345

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL C 202
ChainResidue
CLYS45
CTYR46
CLYS126
CHOH319
CHOH355

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE HYH C 203
ChainResidue
CARG99
CASP101
CLEU103
CASP132
CPHE139
CHOH389

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton donor => ECO:0000305
ChainResidueDetails
AASP101
BASP101
CASP101

site_idSWS_FT_FI2
Number of Residues3
DetailsACT_SITE: Proton acceptor => ECO:0000305
ChainResidueDetails
AASP132
BASP132
CASP132

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 644
ChainResidueDetails
ATYR53electrostatic stabiliser
AASN55electrostatic stabiliser
AARG99electrostatic stabiliser, proton acceptor, proton donor, proton relay
AASP101proton acceptor, proton donor
AASP132activator, proton acceptor, proton donor

site_idMCSA2
Number of Residues5
DetailsM-CSA 644
ChainResidueDetails
BTYR53electrostatic stabiliser
BASN55electrostatic stabiliser
BARG99electrostatic stabiliser, proton acceptor, proton donor, proton relay
BASP101proton acceptor, proton donor
BASP132activator, proton acceptor, proton donor

site_idMCSA3
Number of Residues5
DetailsM-CSA 644
ChainResidueDetails
CTYR53electrostatic stabiliser
CASN55electrostatic stabiliser
CARG99electrostatic stabiliser, proton acceptor, proton donor, proton relay
CASP101proton acceptor, proton donor
CASP132activator, proton acceptor, proton donor

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PDB entries from 2024-10-30

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