3A9I

Crystal structure of homocitrate synthase from Thermus thermophilus complexed with Lys

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004410	molecular_function	homocitrate synthase activity
A	0005737	cellular_component	cytoplasm
A	0009085	biological_process	lysine biosynthetic process
A	0016740	molecular_function	transferase activity
A	0019752	biological_process	carboxylic acid metabolic process
A	0019878	biological_process	lysine biosynthetic process via aminoadipic acid
A	0036440	molecular_function	citrate synthase activity
A	0043436	biological_process	oxoacid metabolic process
A	0046872	molecular_function	metal ion binding
A	0046912	molecular_function	acyltransferase activity, acyl groups converted into alkyl on transfer

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CO A 377

Chain	Residue
A	GLU13
A	HIS195
A	HIS197
A	LYS378
A	HOH406

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site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE LYS A 378

Chain	Residue
A	THR166
A	GLU193
A	HIS195
A	HIS197
A	TYR297
A	CO377
A	HOH406
A	HOH411
A	HOH420
A	HOH429
A	ARG12
A	GLU13
A	ASP92
A	SER135

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Functional Information from PROSITE/UniProt

site_id	PS00815
Number of Residues	17
Details	AIPM_HOMOCIT_SYNTH_1 Alpha-isopropylmalate and homocitrate synthases signature 1. LREGeQfekaNfstqdK

Chain	Residue	Details
A	LEU11-LYS27

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site_id	PS00816
Number of Residues	14
Details	AIPM_HOMOCIT_SYNTH_2 Alpha-isopropylmalate and homocitrate synthases signature 2. IefHgHNDtGcAiA

Chain	Residue	Details
A	ILE192-ALA205

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:19996101

Chain	Residue	Details
A	HIS292

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:19996101, ECO:0007744|PDB:2ZTJ, ECO:0007744|PDB:2ZYF

Chain	Residue	Details
A	ARG12
A	HIS72
A	ARG133

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site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:19996101, ECO:0007744|PDB:2ZYF

Chain	Residue	Details
A	GLU13
A	HIS195
A	HIS197

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site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:19996101, ECO:0007744|PDB:3A9I

Chain	Residue	Details
A	ASP92
A	SER135
A	THR166

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