6LPI

Crystal Structure of AHAS holo-enzyme

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	0005515	molecular_function	protein binding
A	0005948	cellular_component	acetolactate synthase complex
A	0009082	biological_process	branched-chain amino acid biosynthetic process
A	0009099	biological_process	L-valine biosynthetic process
A	0030976	molecular_function	thiamine pyrophosphate binding
A	0050660	molecular_function	flavin adenine dinucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0003984	molecular_function	acetolactate synthase activity
B	0005515	molecular_function	protein binding
B	0005948	cellular_component	acetolactate synthase complex
B	0009082	biological_process	branched-chain amino acid biosynthetic process
B	0009099	biological_process	L-valine biosynthetic process
B	0030976	molecular_function	thiamine pyrophosphate binding
B	0050660	molecular_function	flavin adenine dinucleotide binding
C	0000287	molecular_function	magnesium ion binding
C	0003824	molecular_function	catalytic activity
C	0003984	molecular_function	acetolactate synthase activity
C	0005515	molecular_function	protein binding
C	0005948	cellular_component	acetolactate synthase complex
C	0009082	biological_process	branched-chain amino acid biosynthetic process
C	0009099	biological_process	L-valine biosynthetic process
C	0030976	molecular_function	thiamine pyrophosphate binding
C	0050660	molecular_function	flavin adenine dinucleotide binding
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0003984	molecular_function	acetolactate synthase activity
D	0005515	molecular_function	protein binding
D	0005948	cellular_component	acetolactate synthase complex
D	0009082	biological_process	branched-chain amino acid biosynthetic process
D	0009099	biological_process	L-valine biosynthetic process
D	0030976	molecular_function	thiamine pyrophosphate binding
D	0050660	molecular_function	flavin adenine dinucleotide binding
E	0003984	molecular_function	acetolactate synthase activity
E	0005515	molecular_function	protein binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0005948	cellular_component	acetolactate synthase complex
E	0009082	biological_process	branched-chain amino acid biosynthetic process
E	0009099	biological_process	L-valine biosynthetic process
E	1990610	molecular_function	acetolactate synthase regulator activity
F	0003984	molecular_function	acetolactate synthase activity
F	0005515	molecular_function	protein binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0005948	cellular_component	acetolactate synthase complex
F	0009082	biological_process	branched-chain amino acid biosynthetic process
F	0009099	biological_process	L-valine biosynthetic process
F	1990610	molecular_function	acetolactate synthase regulator activity
G	0003984	molecular_function	acetolactate synthase activity
G	0005515	molecular_function	protein binding
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0005948	cellular_component	acetolactate synthase complex
G	0009082	biological_process	branched-chain amino acid biosynthetic process
G	0009099	biological_process	L-valine biosynthetic process
G	1990610	molecular_function	acetolactate synthase regulator activity
H	0003984	molecular_function	acetolactate synthase activity
H	0005515	molecular_function	protein binding
H	0005737	cellular_component	cytoplasm
H	0005829	cellular_component	cytosol
H	0005948	cellular_component	acetolactate synthase complex
H	0009082	biological_process	branched-chain amino acid biosynthetic process
H	0009099	biological_process	L-valine biosynthetic process
H	1990610	molecular_function	acetolactate synthase regulator activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	27
Details	binding site for residue FAD A 601

Chain	Residue
A	ARG162
A	MET263
A	HIS264
A	GLY283
A	ALA284
A	ARG285
A	ASP287
A	ARG289
A	ALA290
A	ASP307
A	ILE308
A	GLY219
A	ASP309
A	GLU312
A	ALA325
A	ASP326
A	VAL327
A	MET396
A	GLY414
A	GLY415
A	GLY220
A	GLY221
A	THR243
A	LEU244
A	MET245
A	LEU261
A	GLY262

---

site_id	AC2
Number of Residues	24
Details	binding site for residue TPP A 602

Chain	Residue
A	VAL391
A	GLY392
A	GLN393
A	HIS394
A	GLY417
A	MET419
A	GLY443
A	ASP444
A	GLY445
A	SER446
A	MET449
A	ASN471
A	ALA473
A	LEU474
A	GLY475
A	LEU476
A	VAL477
A	MG603
C	PRO35
C	GLY36
C	GLU60
C	CYS83
C	PRO86
C	ASN90

---

site_id	AC3
Number of Residues	5
Details	binding site for residue MG A 603

Chain	Residue
A	ASP444
A	MET469
A	ASN471
A	ALA473
A	TPP602

---

site_id	AC4
Number of Residues	28
Details	binding site for residue FAD B 601

Chain	Residue
B	ARG162
B	GLY219
B	GLY220
B	GLY221
B	THR243
B	LEU244
B	MET245
B	LEU261
B	GLY262
B	MET263
B	HIS264
B	GLY265
B	GLY283
B	ALA284
B	ARG285
B	ASP287
B	ARG289
B	ALA290
B	ASP307
B	ILE308
B	ASP309
B	GLU312
B	ALA325
B	ASP326
B	VAL327
B	MET396
B	GLY414
B	GLY415

---

site_id	AC5
Number of Residues	22
Details	binding site for residue TPP B 602

Chain	Residue
B	VAL477
B	MG603
D	PRO35
D	GLU60
D	CYS83
D	PRO86
D	ASN90
B	VAL391
B	GLY392
B	GLN393
B	HIS394
B	GLY417
B	MET419
B	GLY443
B	ASP444
B	GLY445
B	SER446
B	ASN471
B	ALA473
B	LEU474
B	GLY475
B	LEU476

---

site_id	AC6
Number of Residues	4
Details	binding site for residue MG B 603

Chain	Residue
B	ASP444
B	ASN471
B	ALA473
B	TPP602

---

site_id	AC7
Number of Residues	27
Details	binding site for residue FAD C 601

Chain	Residue
C	ARG162
C	GLY219
C	GLY220
C	GLY221
C	THR243
C	LEU244
C	MET245
C	MET260
C	LEU261
C	MET263
C	HIS264
C	GLY283
C	ALA284
C	ARG285
C	ASP287
C	ARG289
C	ALA290
C	ASP307
C	ILE308
C	ASP309
C	GLU312
C	ALA325
C	ASP326
C	VAL327
C	MET396
C	GLY414
C	GLY415

---

site_id	AC8
Number of Residues	22
Details	binding site for residue TPP C 602

Chain	Residue
A	PRO35
A	GLU60
A	CYS83
A	PRO86
A	ASN90
C	VAL391
C	GLY392
C	GLN393
C	HIS394
C	GLY417
C	MET419
C	GLY443
C	ASP444
C	GLY445
C	SER446
C	ASN471
C	ALA473
C	LEU474
C	GLY475
C	LEU476
C	VAL477
C	MG603

---

site_id	AC9
Number of Residues	4
Details	binding site for residue MG C 603

Chain	Residue
C	ASP444
C	ASN471
C	ALA473
C	TPP602

---

site_id	AD1
Number of Residues	27
Details	binding site for residue FAD D 601

Chain	Residue
D	ARG162
D	GLY219
D	GLY220
D	GLY221
D	THR243
D	LEU244
D	MET245
D	LEU261
D	MET263
D	HIS264
D	GLY283
D	ALA284
D	ARG285
D	ASP287
D	ARG289
D	ALA290
D	ASP307
D	ILE308
D	ASP309
D	GLU312
D	ALA325
D	ASP326
D	VAL327
D	MET396
D	GLY414
D	GLY415
D	LEU476

---

site_id	AD2
Number of Residues	22
Details	binding site for residue TPP D 602

Chain	Residue
B	PRO35
B	GLU60
B	PRO86
B	ASN90
B	GLN123
D	VAL391
D	GLY392
D	GLN393
D	HIS394
D	GLY417
D	MET419
D	GLY443
D	ASP444
D	GLY445
D	SER446
D	ASN471
D	ALA473
D	LEU474
D	GLY475
D	LEU476
D	VAL477
D	MG603

---

site_id	AD3
Number of Residues	5
Details	binding site for residue MG D 603

Chain	Residue
D	ASP444
D	MET469
D	ASN471
D	ALA473
D	TPP602

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE427-SER446

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	292
Details	Domain: {"description":"ACT","evidences":[{"source":"PROSITE-ProRule","id":"PRU01007","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	320
Details	Region: {"description":"Thiamine pyrophosphate binding"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	176
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---