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5NX7

Crystal structure of 1,8-cineole synthase from Streptomyces clavuligerus in complex with 2-fluoroneryl diphosphate and 2-fluorogeranyl diphosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0016829molecular_functionlyase activity
A0033383biological_processgeranyl diphosphate metabolic process
A0046872molecular_functionmetal ion binding
A0102313molecular_function1,8-cineole synthase activity
B0000287molecular_functionmagnesium ion binding
B0016829molecular_functionlyase activity
B0033383biological_processgeranyl diphosphate metabolic process
B0046872molecular_functionmetal ion binding
B0102313molecular_function1,8-cineole synthase activity
Functional Information from PDB Data
site_idAC1
Number of Residues21
Detailsbinding site for residue 0FV A 400
ChainResidue
APHE77
AARG314
ATYR315
ALA6401
AMG402
AMG403
AMG404
AHOH502
AHOH533
AHOH544
AHOH560
AARG174
AHOH562
AHOH572
ALEU183
AASN220
ASER224
ALYS227
AGLU228
AASN305
ATRP308

site_idAC2
Number of Residues26
Detailsbinding site for residue LA6 A 401
ChainResidue
APHE77
APHE78
AASP81
AARG174
APHE179
AMET180
AILE216
AASN217
AASN220
ASER224
ALYS227
AGLU228
AASN305
AARG314
ATYR315
A0FV400
AMG402
AMG403
AMG404
AHOH502
AHOH533
AHOH535
AHOH544
AHOH568
AHOH572
AHOH591

site_idAC3
Number of Residues6
Detailsbinding site for residue MG A 402
ChainResidue
AASN220
ASER224
AGLU228
A0FV400
ALA6401
AHOH533

site_idAC4
Number of Residues7
Detailsbinding site for residue MG A 403
ChainResidue
AASP81
A0FV400
ALA6401
AMG404
AHOH535
AHOH568
AHOH572

site_idAC5
Number of Residues8
Detailsbinding site for residue MG A 404
ChainResidue
AASP81
A0FV400
ALA6401
AMG403
AHOH502
AHOH504
AHOH560
AHOH568

site_idAC6
Number of Residues5
Detailsbinding site for residue 9D2 A 405
ChainResidue
AGLU6
AGLN250
ALEU253
AARG257
BGLU43

site_idAC7
Number of Residues7
Detailsbinding site for residue NDS A 406
ChainResidue
APHE19
AARG22
AARG26
AGLN63
AGLY64
BPRO18
BARG22

site_idAC8
Number of Residues23
Detailsbinding site for residue 0FV B 400
ChainResidue
BHOH520
BHOH524
BHOH543
BHOH619
BPHE77
BPHE78
BASP81
BARG174
BPHE179
BLEU183
BILE216
BASN220
BSER224
BLYS227
BGLU228
BASN305
BARG314
BTYR315
BLA6401
BMG402
BMG403
BMG404
BHOH511

site_idAC9
Number of Residues28
Detailsbinding site for residue LA6 B 401
ChainResidue
BPHE77
BPHE78
BASP81
BARG174
BPHE179
BMET180
BILE216
BASN217
BASN220
BSER224
BLYS227
BGLU228
BASN305
BTRP308
BARG314
BTYR315
B0FV400
BMG402
BMG403
BMG404
BHOH511
BHOH520
BHOH524
BHOH531
BHOH536
BHOH543
BHOH587
BHOH619

site_idAD1
Number of Residues6
Detailsbinding site for residue MG B 402
ChainResidue
BASN220
BSER224
BGLU228
B0FV400
BLA6401
BHOH520

site_idAD2
Number of Residues7
Detailsbinding site for residue MG B 403
ChainResidue
BASP81
B0FV400
BLA6401
BMG404
BHOH531
BHOH536
BHOH619

site_idAD3
Number of Residues8
Detailsbinding site for residue MG B 404
ChainResidue
BASP81
B0FV400
BLA6401
BMG403
BHOH504
BHOH511
BHOH524
BHOH536

site_idAD4
Number of Residues6
Detailsbinding site for residue 9D2 B 405
ChainResidue
AGLU43
BGLU6
BGLN250
BLEU253
BARG257
BHOH509

site_idAD5
Number of Residues6
Detailsbinding site for residue NDS B 406
ChainResidue
APRO18
BPHE19
BARG22
BARG26
BGLN63
BGLY64

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:28966840, ECO:0007744|PDB:5NX6, ECO:0007744|PDB:5NX7
ChainResidueDetails
AASP81
BLYS227
BGLU228
BARG314
AASN220
ASER224
ALYS227
AGLU228
AARG314
BASP81
BASN220
BSER224

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:28966840, ECO:0007744|PDB:5NX7
ChainResidueDetails
AARG174
BARG174

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PDB entries from 2024-07-10

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