5K6Q

Crystal structure of Arabidopsis thaliana acetohydroxyacid synthase catalytic subunit

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0003984	molecular_function	acetolactate synthase activity
A	0009082	biological_process	branched-chain amino acid biosynthetic process
A	0030976	molecular_function	thiamine pyrophosphate binding
A	0050660	molecular_function	flavin adenine dinucleotide binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue MG A 701

Chain	Residue
A	ASP538
A	ASN565
A	HIS567
A	TDM704
A	HOH876

---

site_id	AC2
Number of Residues	34
Details	binding site for residue FAD A 702

Chain	Residue
A	GLY309
A	THR331
A	LEU332
A	MET333
A	LEU349
A	GLY350
A	MET351
A	HIS352
A	GLY371
A	VAL372
A	ARG373
A	ASP375
A	ARG377
A	VAL378
A	ASP395
A	ILE396
A	ASP397
A	GLU400
A	GLY413
A	ASP414
A	VAL415
A	GLN489
A	MET490
A	SER507
A	GLY508
A	GLY509
A	HOH803
A	HOH839
A	HOH860
A	HOH865
A	PHE206
A	ARG246
A	GLY307
A	GLY308

---

site_id	AC3
Number of Residues	6
Details	binding site for residue NHE A 703

Chain	Residue
A	LYS220
A	HIS221
A	LEU273
A	PRO274
A	GLY275
A	TYR276

---

site_id	AC4
Number of Residues	25
Details	binding site for residue TDM A 704

Chain	Residue
A	TYR118
A	PRO119
A	GLU144
A	PRO170
A	ASN174
A	GLN207
A	VAL485
A	GLY486
A	GLN487
A	HIS488
A	GLY511
A	MET513
A	GLY537
A	ASP538
A	GLY539
A	SER540
A	ASN565
A	HIS567
A	LEU568
A	GLY569
A	MET570
A	VAL571
A	MG701
A	HOH824
A	HOH876

---

Functional Information from PROSITE/UniProt

site_id	PS00187
Number of Residues	20
Details	TPP_ENZYMES Thiamine pyrophosphate enzymes signature. IGasvanPdaivVdIdGDGS

Chain	Residue	Details
A	ILE521-SER540

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:16407096

Chain	Residue	Details
A	GLU144
A	GLN207
A	ARG246
A	ASP414

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:32640464, ECO:0007744|PDB:6U9H

Chain	Residue	Details
A	SER186
A	GLN487

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:16407096, ECO:0007744|PDB:1Z8N

Chain	Residue	Details
A	LYS220

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:16407096, ECO:0007744|PDB:1YBH

Chain	Residue	Details
A	LYS256
A	ASP376
A	TRP574
A	SER653

---

site_id	SWS_FT_FI5
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:16407096, ECO:0000269|PubMed:32640464, ECO:0007744|PDB:6U9H

Chain	Residue	Details
A	GLY308
A	THR331
A	LEU349
A	GLY371
A	ASP395
A	GLY508

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:32640464, ECO:0007744|PDB:6VZ8

Chain	Residue	Details
A	GLY511

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:16407096, ECO:0000269|PubMed:19187232, ECO:0000269|PubMed:32640464, ECO:0007744|PDB:6U9H

Chain	Residue	Details
A	ASP538

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:16407096, ECO:0000269|PubMed:19187232

Chain	Residue	Details
A	ASN565

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:16407096, ECO:0000269|PubMed:19187232, ECO:0000269|PubMed:32640464, ECO:0007744|PDB:6VZ8

Chain	Residue	Details
A	HIS567

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Cysteine sulfinic acid (-SO2H) => ECO:0000269|PubMed:16407096, ECO:0000269|PubMed:19187232

Chain	Residue	Details
A	CSD340

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