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1NU3

Limonene-1,2-epoxide hydrolase in complex with valpromide

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
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MES A 3001
ChainResidue
AASP50
ATHR51
ATHR128
AHOH4153
BARG9
BASP50
BTHR51
BGLY63

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE VPR A 4001
ChainResidue
AARG99
AASP101
ALEU103
AASP132
AHOH4013
AILE80

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE VPR B 5001
ChainResidue
BILE80
BARG99
BASP101
BLEU103
BASP132
BPHE134
BHOH5059

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305
ChainResidueDetails
AVAL102
BVAL102

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305
ChainResidueDetails
ATYR133
BTYR133

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 12773375
ChainResidueDetails
AARG99
AASP101
AASP132

site_idCSA2
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 12773375
ChainResidueDetails
BARG99
BASP101
BASP132

site_idMCSA1
Number of Residues5
DetailsM-CSA 644
ChainResidueDetails
AGLN54electrostatic stabiliser
AMSE56electrostatic stabiliser
AVAL100electrostatic stabiliser, proton acceptor, proton donor, proton relay
AVAL102proton acceptor, proton donor
ATYR133activator, proton acceptor, proton donor

site_idMCSA2
Number of Residues5
DetailsM-CSA 644
ChainResidueDetails
BGLN54electrostatic stabiliser
BMSE56electrostatic stabiliser
BVAL100electrostatic stabiliser, proton acceptor, proton donor, proton relay
BVAL102proton acceptor, proton donor
BTYR133activator, proton acceptor, proton donor

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PDB entries from 2024-06-26

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