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6AXU

W203Y Epi-isozizaene synthase

Functional Information from GO Data
ChainGOidnamespacecontents
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
A0052680molecular_functionepi-isozizaene synthase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue BTM A 401
ChainResidue
APHE95
APHE96
ATHR197
APHE198
AASN240
AHIS333
ATYR339
APOP402

site_idAC2
Number of Residues19
Detailsbinding site for residue POP A 402
ChainResidue
AARG194
AASN240
ASER244
ALYS247
AGLU248
AARG338
ATYR339
ABTM401
AMG403
AMG404
AMG405
AHOH508
AHOH513
AHOH560
AHOH563
AHOH583
AHOH587
AHOH631
AASP99

site_idAC3
Number of Residues5
Detailsbinding site for residue MG A 403
ChainResidue
AASN240
ASER244
AGLU248
APOP402
AHOH583

site_idAC4
Number of Residues6
Detailsbinding site for residue MG A 404
ChainResidue
AASP99
APOP402
AMG405
AHOH563
AHOH587
AHOH631

site_idAC5
Number of Residues7
Detailsbinding site for residue MG A 405
ChainResidue
AASP99
APOP402
AMG404
AHOH503
AHOH513
AHOH560
AHOH563

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING:
ChainResidueDetails
AASP99
AASP103
AASN240
ASER244
AGLU248

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 263
ChainResidueDetails
APHE95electrostatic stabiliser, polar/non-polar interaction, steric role
APHE96electrostatic stabiliser, polar/non-polar interaction, steric role
APHE198electrostatic stabiliser, polar/non-polar interaction, steric role
AARG338electrostatic stabiliser, hydrogen bond donor, promote heterolysis

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PDB entries from 2024-07-24

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