1C97

S642A:ISOCITRATE COMPLEX OF ACONITASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003994	molecular_function	aconitate hydratase activity
A	0005506	molecular_function	iron ion binding
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0006099	biological_process	tricarboxylic acid cycle
A	0006101	biological_process	citrate metabolic process
A	0008198	molecular_function	ferrous iron binding
A	0016829	molecular_function	lyase activity
A	0046872	molecular_function	metal ion binding
A	0051538	molecular_function	3 iron, 4 sulfur cluster binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SF4 A 755

Chain	Residue
A	HIS101
A	O1500
A	HIS167
A	SER357
A	CYS358
A	CYS421
A	CYS424
A	ILE425
A	ASN446
A	ICT756

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE O A 1500

Chain	Residue
A	ASP165
A	HIS167
A	SF4755
A	ICT756

---

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ICT A 756

Chain	Residue
A	GLN72
A	ALA74
A	THR75
A	HIS101
A	ASP165
A	SER166
A	ARG447
A	ARG452
A	ARG580
A	ALA642
A	SER643
A	ARG644
A	SF4755
A	O1500

---

Functional Information from PROSITE/UniProt

site_id	PS00099
Number of Residues	14
Details	THIOLASE_3 Thiolases active site. GLGGICIGvGgAdA

Chain	Residue	Details
A	GLY173-ALA186

---

site_id	PS00450
Number of Residues	17
Details	ACONITASE_1 Aconitase family signature 1. IrvGlIGSC.TNSsyedM

Chain	Residue	Details
A	ILE350-MET366

---

site_id	PS01244
Number of Residues	14
Details	ACONITASE_2 Aconitase family signature 2. GgiVlanACGPCIG

Chain	Residue	Details
A	GLY413-GLY426

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:1547214, ECO:0007744|PDB:8ACN

Chain	Residue	Details
A	GLN72
A	ASP165
A	ARG447
A	ARG452
A	ARG580
A	SER643

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:1547214, ECO:0000269|PubMed:3372519, ECO:0007744|PDB:8ACN

Chain	Residue	Details
A	CYS358
A	CYS421
A	CYS424

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q99KI0

Chain	Residue	Details
A	LYS4
A	LYS384
A	LYS522
A	LYS564
A	LYS601
A	LYS662

---

site_id	SWS_FT_FI4
Number of Residues	10
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KI0

Chain	Residue	Details
A	LYS23
A	LYS703
A	LYS111
A	LYS117
A	LYS206
A	LYS490
A	LYS496
A	LYS546
A	LYS578
A	LYS696

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q99798

Chain	Residue	Details
A	SER532

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q99KI0

Chain	Residue	Details
A	SER643

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q99KI0

Chain	Residue	Details
A	LYS709
A	LYS716

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	7
Details	Annotated By Reference To The Literature 1fgh

Chain	Residue	Details
A	ALA642
A	GLU262
A	ASP100
A	HIS147
A	HIS101
A	HIS167
A	ASP165

---

site_id	MCSA1
Number of Residues	6
Details	M-CSA 552

Chain	Residue	Details
A	ASP100	electrostatic stabiliser, increase acidity
A	HIS101	electrostatic stabiliser, proton acceptor, proton donor
A	ASP165	electrostatic stabiliser
A	ARG447	electrostatic stabiliser
A	ALA642	proton acceptor, proton donor
A	ARG644	electrostatic stabiliser

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