Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5YPP

Crystal structure of IlvN.Val-1a

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003984	molecular_function	acetolactate synthase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005948	cellular_component	acetolactate synthase complex
A	0008652	biological_process	amino acid biosynthetic process
A	0009082	biological_process	branched-chain amino acid biosynthetic process
A	0009097	biological_process	isoleucine biosynthetic process
A	0009099	biological_process	L-valine biosynthetic process
A	0016740	molecular_function	transferase activity
A	1990610	molecular_function	acetolactate synthase regulator activity
B	0003984	molecular_function	acetolactate synthase activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005948	cellular_component	acetolactate synthase complex
B	0008652	biological_process	amino acid biosynthetic process
B	0009082	biological_process	branched-chain amino acid biosynthetic process
B	0009097	biological_process	isoleucine biosynthetic process
B	0009099	biological_process	L-valine biosynthetic process
B	0016740	molecular_function	transferase activity
B	1990610	molecular_function	acetolactate synthase regulator activity
C	0003984	molecular_function	acetolactate synthase activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005948	cellular_component	acetolactate synthase complex
C	0008652	biological_process	amino acid biosynthetic process
C	0009082	biological_process	branched-chain amino acid biosynthetic process
C	0009097	biological_process	isoleucine biosynthetic process
C	0009099	biological_process	L-valine biosynthetic process
C	0016740	molecular_function	transferase activity
C	1990610	molecular_function	acetolactate synthase regulator activity
D	0003984	molecular_function	acetolactate synthase activity
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005948	cellular_component	acetolactate synthase complex
D	0008652	biological_process	amino acid biosynthetic process
D	0009082	biological_process	branched-chain amino acid biosynthetic process
D	0009097	biological_process	isoleucine biosynthetic process
D	0009099	biological_process	L-valine biosynthetic process
D	0016740	molecular_function	transferase activity
D	1990610	molecular_function	acetolactate synthase regulator activity
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	0008652	biological_process	amino acid biosynthetic process
E	0009082	biological_process	branched-chain amino acid biosynthetic process
E	0009097	biological_process	isoleucine biosynthetic process
E	0009099	biological_process	L-valine biosynthetic process
E	0016740	molecular_function	transferase activity
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	0008652	biological_process	amino acid biosynthetic process
F	0009082	biological_process	branched-chain amino acid biosynthetic process
F	0009097	biological_process	isoleucine biosynthetic process
F	0009099	biological_process	L-valine biosynthetic process
F	0016740	molecular_function	transferase activity
F	1990610	molecular_function	acetolactate synthase regulator activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	binding site for residue VAL A 101

Chain	Residue
A	ASN19
A	HIS20
A	GLY22
A	VAL23
A	MET24
A	HOH205
A	HOH207
B	ASN37
B	VAL38

site_id	AC2
Number of Residues	10
Details	binding site for residue VAL A 102

Chain	Residue
A	ASN37
A	VAL38
A	HOH209
B	ASN19
B	HIS20
B	GLY22
B	VAL23
B	MET24
B	CYS43
B	HOH213

site_id	AC3
Number of Residues	8
Details	binding site for residue PEG A 103

Chain	Residue
A	LEU57
A	PRO87
A	THR88
A	MET89
A	PHE90
A	ASN91
A	HOH210
B	PRO45

site_id	AC4
Number of Residues	4
Details	binding site for residue PEG B 101

Chain	Residue
A	PHE97
B	PHE96
B	HOH205
D	VAL95

site_id	AC5
Number of Residues	6
Details	binding site for residue PEG B 102

Chain	Residue
B	LEU57
B	PRO87
B	THR88
B	MET89
B	PHE90
B	ASN91

site_id	AC6
Number of Residues	10
Details	binding site for residue VAL C 101

Chain	Residue
C	ASN19
C	HIS20
C	GLY22
C	VAL23
C	MET24
C	CYS43
C	HOH212
D	ASN37
D	VAL38
D	HOH204

site_id	AC7
Number of Residues	10
Details	binding site for residue VAL C 102

Chain	Residue
C	ASN37
C	VAL38
C	HOH203
C	HOH206
D	ASN19
D	HIS20
D	GLY22
D	VAL23
D	MET24
D	CYS43

site_id	AC8
Number of Residues	2
Details	binding site for residue PEG C 103

Chain	Residue
C	PHE96
C	PHE97

site_id	AC9
Number of Residues	8
Details	binding site for residue PEG C 104

Chain	Residue
C	LEU57
C	PRO87
C	THR88
C	MET89
C	PHE90
C	ASN91
C	HOH202
D	PRO45

site_id	AD1
Number of Residues	8
Details	binding site for residue PEG D 101

Chain	Residue
C	LEU44
C	PRO45
D	LEU57
D	PHE90
D	ASN91
D	ALA94
D	GLN98
D	HOH210

site_id	AD2
Number of Residues	11
Details	binding site for residue VAL E 101

Chain	Residue
E	ASN19
E	HIS20
E	PRO21
E	GLY22
E	VAL23
E	MET24
E	CYS43
E	HOH207
E	HOH209
F	ASN37
F	VAL38

site_id	AD3
Number of Residues	8
Details	binding site for residue PEG E 102

Chain	Residue
E	LEU57
E	PRO87
E	THR88
E	MET89
E	PHE90
E	ASN91
E	HOH208
F	PRO45

site_id	AD4
Number of Residues	10
Details	binding site for residue VAL F 101

Chain	Residue
F	VAL23
F	MET24
F	CYS43
F	HOH207
F	HOH208
E	ASN37
E	VAL38
F	ASN19
F	HIS20
F	GLY22

site_id	AD5
Number of Residues	4
Details	binding site for residue ACT F 102

Chain	Residue
F	ARG82
F	ASN83
F	GLN84
F	HOH206

site_id	AD6
Number of Residues	3
Details	binding site for residue PEG F 103

Chain	Residue
E	PHE96
E	PHE97
F	PHE97

site_id	AD7
Number of Residues	8
Details	binding site for residue PEG F 104

Chain	Residue
E	PRO45
F	ASN10
F	LEU57
F	PRO87
F	PHE90
F	ASN91
F	HOH202
F	HOH205

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)