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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3LZ9

The Crystal Structure of 5-epi-aristolochene synthase M4 mutant complexed with (2-trans,6-trans)-2-fluorofarnesyl diphosphate

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	18
Details	BINDING SITE FOR RESIDUE FPF A 700

Chain	Residue
A	ARG264
A	TYR520
A	HOH549
A	HOH550
A	HOH551
A	HOH552
A	HOH553
A	MG852
A	MG853
A	MG854
A	TRP273
A	SER298
A	ASP301
A	ASP305
A	THR402
A	THR403
A	LEU407
A	ASP444

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 852

Chain	Residue
A	ASP301
A	ASP305
A	GLU379
A	HOH552
A	FPF700

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 853

Chain	Residue
A	ASP301
A	ASP305
A	HOH553
A	FPF700

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG A 854

Chain	Residue
A	ASP444
A	THR448
A	GLU452
A	HOH549
A	HOH550
A	HOH554
A	FPF700

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

227111

PDB entries from 2024-11-06

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