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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5ILI

Tobacco 5-epi-aristolochene synthase with CAPSO buffer molecule and Mg2+ ions

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0005737	cellular_component	cytoplasm
A	0008299	biological_process	isoprenoid biosynthetic process
A	0010333	molecular_function	terpene synthase activity
A	0016102	biological_process	diterpenoid biosynthetic process
A	0016114	biological_process	terpenoid biosynthetic process
A	0016829	molecular_function	lyase activity
A	0016838	molecular_function	carbon-oxygen lyase activity, acting on phosphates
A	0046872	molecular_function	metal ion binding
A	0051762	biological_process	sesquiterpene biosynthetic process
A	0102698	molecular_function	5-epi-aristolochene synthase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue MG A 601

Chain	Residue
A	ASP444
A	THR448
A	GLU452
A	3FX603
A	HOH701
A	HOH730
A	HOH829

site_id	AC2
Number of Residues	6
Details	binding site for residue MG A 602

Chain	Residue
A	3CX604
A	HOH709
A	HOH734
A	HOH826
A	ASP301
A	3FX603

site_id	AC3
Number of Residues	13
Details	binding site for residue 3FX A 603

Chain	Residue
A	THR401
A	THR402
A	THR403
A	ARG441
A	ASP444
A	TYR527
A	MG601
A	MG602
A	3CX604
A	HOH701
A	HOH709
A	HOH717
A	HOH829

site_id	AC4
Number of Residues	13
Details	binding site for residue 3CX A 604

Chain	Residue
A	TRP273
A	THR401
A	THR402
A	ARG441
A	ASP444
A	TYR520
A	TYR527
A	MG602
A	3FX603
A	HOH701
A	HOH709
A	HOH717
A	HOH829

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: 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

Chain	Residue	Details
A	ARG264

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: 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

Chain	Residue	Details
A	ASP301

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: 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

Chain	Residue	Details
A	ASP305

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: 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

Chain	Residue	Details
A	ARG441

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: 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

Chain	Residue	Details
A	ASP444
A	GLU452

site_id	SWS_FT_FI6
Number of Residues	1
Details	BINDING: 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

Chain	Residue	Details
A	ASP445

site_id	SWS_FT_FI7
Number of Residues	1
Details	BINDING: 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

Chain	Residue	Details
A	THR448

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	10
Details	M-CSA 265

Chain	Residue	Details
A	ARG264	electrostatic stabiliser, hydrogen bond donor, promote heterolysis
A	TYR527	electrostatic stabiliser, polar interaction
A	TRP273	electrostatic stabiliser, hydrogen bond donor, polar interaction, proton acceptor, proton donor
A	THR401	electrostatic stabiliser, polar interaction
A	THR402	electrostatic stabiliser, polar interaction
A	THR403	electrostatic stabiliser, polar interaction
A	ARG441	electrostatic stabiliser, hydrogen bond donor, promote heterolysis
A	ASP444	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	TYR520	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
A	ASP525	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

223166

PDB entries from 2024-07-31

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