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1HXC

CRYSTAL STRUCTURE OF TEAS C440W

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005737cellular_componentcytoplasm
A0006720biological_processisoprenoid metabolic process
A0010333molecular_functionterpene synthase activity
A0016102biological_processditerpenoid biosynthetic process
A0016114biological_processterpenoid biosynthetic process
A0016829molecular_functionlyase activity
A0016838molecular_functioncarbon-oxygen lyase activity, acting on phosphates
A0046872molecular_functionmetal ion binding
A0051762biological_processsesquiterpene biosynthetic process
A0102698molecular_function5-epi-aristolochene synthase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE FHP A 900
ChainResidue
AARG266
ATHR403
ACYS270
AILE294
AASP301
AASP305
ATYR376
AGLU379
ATHR401
ATHR402

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:20175559, ECO:0000269|PubMed:27328867, ECO:0000305|PubMed:25897591, ECO:0000305|PubMed:9295271, ECO:0000305|Ref.13, ECO:0000305|Ref.9, ECO:0007744|PDB:3LZ9, ECO:0007744|PDB:3M00, ECO:0007744|PDB:3M01, ECO:0007744|PDB:3M02, ECO:0007744|PDB:4DI5, ECO:0007744|PDB:4RNQ, ECO:0007744|PDB:5EAT, ECO:0007744|PDB:5EAU, ECO:0007744|PDB:5IK0, ECO:0007744|PDB:5IK6, ECO:0007744|PDB:5IK9, ECO:0007744|PDB:5IKA, ECO:0007744|PDB:5IKH, ECO:0007744|PDB:5IL8, ECO:0007744|PDB:5ILD, ECO:0007744|PDB:5ILY
ChainResidueDetails
AARG264

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:20175559, ECO:0000269|PubMed:25897591, ECO:0000269|PubMed:26378620, ECO:0000269|PubMed:27328867, ECO:0000269|PubMed:9295271, ECO:0007744|PDB:3LZ9, ECO:0007744|PDB:3M00, ECO:0007744|PDB:3M01, ECO:0007744|PDB:3M02, ECO:0007744|PDB:4RNQ, ECO:0007744|PDB:5DHI, ECO:0007744|PDB:5EAT, ECO:0007744|PDB:5IK0, ECO:0007744|PDB:5IK9, ECO:0007744|PDB:5IKA
ChainResidueDetails
AASP301

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:20175559, ECO:0000269|PubMed:25897591, ECO:0000269|PubMed:26378620, ECO:0000269|PubMed:27328867, ECO:0000269|PubMed:9295271, ECO:0007744|PDB:1HXA, ECO:0007744|PDB:3LZ9, ECO:0007744|PDB:3M00, ECO:0007744|PDB:3M01, ECO:0007744|PDB:3M02, ECO:0007744|PDB:4RNQ, ECO:0007744|PDB:5DHI, ECO:0007744|PDB:5DHK, ECO:0007744|PDB:5EAT, ECO:0007744|PDB:5IK0, ECO:0007744|PDB:5IK9, ECO:0007744|PDB:5IKA
ChainResidueDetails
AASP305

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:27328867, ECO:0000305|PubMed:20175559, ECO:0000305|PubMed:25897591, ECO:0000305|PubMed:27328867, ECO:0000305|Ref.13, ECO:0000305|Ref.7, ECO:0000305|Ref.9, ECO:0007744|PDB:1HXA, ECO:0007744|PDB:1HXC, ECO:0007744|PDB:3M02, ECO:0007744|PDB:4DI5, ECO:0007744|PDB:4RNQ, ECO:0007744|PDB:5IK0, ECO:0007744|PDB:5IK6, ECO:0007744|PDB:5IKA, ECO:0007744|PDB:5IL3, ECO:0007744|PDB:5ILH, ECO:0007744|PDB:5ILI, ECO:0007744|PDB:5ILY
ChainResidueDetails
AARG441

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:20175559, ECO:0000269|PubMed:25897591, ECO:0000269|PubMed:26378620, ECO:0000269|PubMed:27328867, ECO:0000269|PubMed:9295271, ECO:0000269|Ref.13, ECO:0000269|Ref.7, ECO:0000269|Ref.9, ECO:0007744|PDB:1HX9, ECO:0007744|PDB:1HXA, ECO:0007744|PDB:3LZ9, ECO:0007744|PDB:3M00, ECO:0007744|PDB:3M01, ECO:0007744|PDB:3M02, ECO:0007744|PDB:4DI5, ECO:0007744|PDB:4RNQ, ECO:0007744|PDB:5DHI, ECO:0007744|PDB:5EAS, ECO:0007744|PDB:5EAT, ECO:0007744|PDB:5EAU, ECO:0007744|PDB:5IK0, ECO:0007744|PDB:5IK6, ECO:0007744|PDB:5IK9, ECO:0007744|PDB:5IKA, ECO:0007744|PDB:5IKH, ECO:0007744|PDB:5IL3, ECO:0007744|PDB:5ILD, ECO:0007744|PDB:5ILI, ECO:0007744|PDB:5ILY
ChainResidueDetails
AASP444
AGLU452

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:20175559, ECO:0000269|PubMed:25897591, ECO:0000269|PubMed:27328867, ECO:0000269|PubMed:9295271, ECO:0000269|Ref.13, ECO:0000269|Ref.9, ECO:0007744|PDB:3M02, ECO:0007744|PDB:4DI5, ECO:0007744|PDB:4RNQ, ECO:0007744|PDB:5EAS, ECO:0007744|PDB:5EAT, ECO:0007744|PDB:5IKH, ECO:0007744|PDB:5ILD
ChainResidueDetails
AASP445

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:20175559, ECO:0000269|PubMed:25897591, ECO:0000269|PubMed:26378620, ECO:0000269|PubMed:27328867, ECO:0000269|PubMed:9295271, ECO:0000269|Ref.13, ECO:0000269|Ref.7, ECO:0000269|Ref.9, ECO:0007744|PDB:1HX9, ECO:0007744|PDB:1HXA, ECO:0007744|PDB:3LZ9, ECO:0007744|PDB:3M00, ECO:0007744|PDB:3M01, ECO:0007744|PDB:3M02, ECO:0007744|PDB:4DI5, ECO:0007744|PDB:4RNQ, ECO:0007744|PDB:5DHI, ECO:0007744|PDB:5EAS, ECO:0007744|PDB:5EAT, ECO:0007744|PDB:5EAU, ECO:0007744|PDB:5IK9, ECO:0007744|PDB:5IKA, ECO:0007744|PDB:5IKH, ECO:0007744|PDB:5ILD, ECO:0007744|PDB:5ILI, ECO:0007744|PDB:5ILY
ChainResidueDetails
ATHR448

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1n20
ChainResidueDetails
ATRP273

site_idCSA2
Number of Residues8
DetailsAnnotated By Reference To The Literature 1n20
ChainResidueDetails
AARG441
ATHR401
ATHR403
ATRP273
AARG264
AASP444
ATYR520
ATHR402

site_idMCSA1
Number of Residues10
DetailsM-CSA 265
ChainResidueDetails
AARG264electrostatic stabiliser, hydrogen bond donor, promote heterolysis
ATYR527electrostatic stabiliser, polar interaction
ATRP273electrostatic stabiliser, hydrogen bond donor, polar interaction, proton acceptor, proton donor
ATHR401electrostatic stabiliser, polar interaction
ATHR402electrostatic stabiliser, polar interaction
ATHR403electrostatic stabiliser, polar interaction
AARG441electrostatic stabiliser, hydrogen bond donor, promote heterolysis
AASP444hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ATYR520hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
AASP525hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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PDB entries from 2024-08-28

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