Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3VAV

Crystal structure of 3-methyl-2-oxobutanoate hydroxymethyltransferase from Burkholderia thailandensis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0003864	molecular_function	3-methyl-2-oxobutanoate hydroxymethyltransferase activity
A	0005737	cellular_component	cytoplasm
A	0015940	biological_process	pantothenate biosynthetic process
A	0016740	molecular_function	transferase activity
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0003864	molecular_function	3-methyl-2-oxobutanoate hydroxymethyltransferase activity
B	0005737	cellular_component	cytoplasm
B	0015940	biological_process	pantothenate biosynthetic process
B	0016740	molecular_function	transferase activity
B	0046872	molecular_function	metal ion binding
C	0000287	molecular_function	magnesium ion binding
C	0003824	molecular_function	catalytic activity
C	0003864	molecular_function	3-methyl-2-oxobutanoate hydroxymethyltransferase activity
C	0005737	cellular_component	cytoplasm
C	0015940	biological_process	pantothenate biosynthetic process
C	0016740	molecular_function	transferase activity
C	0046872	molecular_function	metal ion binding
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0003864	molecular_function	3-methyl-2-oxobutanoate hydroxymethyltransferase activity
D	0005737	cellular_component	cytoplasm
D	0015940	biological_process	pantothenate biosynthetic process
D	0016740	molecular_function	transferase activity
D	0046872	molecular_function	metal ion binding
E	0000287	molecular_function	magnesium ion binding
E	0003824	molecular_function	catalytic activity
E	0003864	molecular_function	3-methyl-2-oxobutanoate hydroxymethyltransferase activity
E	0005737	cellular_component	cytoplasm
E	0015940	biological_process	pantothenate biosynthetic process
E	0016740	molecular_function	transferase activity
E	0046872	molecular_function	metal ion binding
F	0000287	molecular_function	magnesium ion binding
F	0003824	molecular_function	catalytic activity
F	0003864	molecular_function	3-methyl-2-oxobutanoate hydroxymethyltransferase activity
F	0005737	cellular_component	cytoplasm
F	0015940	biological_process	pantothenate biosynthetic process
F	0016740	molecular_function	transferase activity
F	0046872	molecular_function	metal ion binding
G	0000287	molecular_function	magnesium ion binding
G	0003824	molecular_function	catalytic activity
G	0003864	molecular_function	3-methyl-2-oxobutanoate hydroxymethyltransferase activity
G	0005737	cellular_component	cytoplasm
G	0015940	biological_process	pantothenate biosynthetic process
G	0016740	molecular_function	transferase activity
G	0046872	molecular_function	metal ion binding
H	0000287	molecular_function	magnesium ion binding
H	0003824	molecular_function	catalytic activity
H	0003864	molecular_function	3-methyl-2-oxobutanoate hydroxymethyltransferase activity
H	0005737	cellular_component	cytoplasm
H	0015940	biological_process	pantothenate biosynthetic process
H	0016740	molecular_function	transferase activity
H	0046872	molecular_function	metal ion binding
I	0000287	molecular_function	magnesium ion binding
I	0003824	molecular_function	catalytic activity
I	0003864	molecular_function	3-methyl-2-oxobutanoate hydroxymethyltransferase activity
I	0005737	cellular_component	cytoplasm
I	0015940	biological_process	pantothenate biosynthetic process
I	0016740	molecular_function	transferase activity
I	0046872	molecular_function	metal ion binding
J	0000287	molecular_function	magnesium ion binding
J	0003824	molecular_function	catalytic activity
J	0003864	molecular_function	3-methyl-2-oxobutanoate hydroxymethyltransferase activity
J	0005737	cellular_component	cytoplasm
J	0015940	biological_process	pantothenate biosynthetic process
J	0016740	molecular_function	transferase activity
J	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 272

Chain	Residue
A	ASP71
A	ASP72
A	TYR75
A	HOH762
F	TYR75

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO B 272

Chain	Residue
B	TYR75
B	ARG82
G	GLN60
G	HOH452

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 272

Chain	Residue
C	LYS120
C	HIS144
C	VAL222
C	HOH286
C	HOH465
C	HOH1168

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO D 272

Chain	Residue
D	TYR75
D	ALA78
D	ARG82
I	HOH296

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO E 272

Chain	Residue
E	LYS120
E	HIS144
E	HOH433
E	HOH751

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO G 272

Chain	Residue
B	GLN60
G	ARG82
G	HOH281
G	HOH295

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO G 273

Chain	Residue
G	LYS120
G	HIS144
G	VAL222
G	HOH282
G	HOH1183
G	HOH1692

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO H 272

Chain	Residue
C	GLN60
H	ARG82
H	HOH331

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO I 272

Chain	Residue
I	LYS120
I	HIS144
I	HOH279
I	HOH1195

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL I 273

Chain	Residue
D	HOH648
I	HOH1794

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO J 272

Chain	Residue
E	GLN60
J	TYR75
J	ARG82
J	HOH457

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO J 273

Chain	Residue
J	LYS120
J	HOH289
J	HOH1906
J	HOH2469

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	ACT_SITE: Proton acceptor => ECO:0000255\|HAMAP-Rule:MF_00156

Chain	Residue	Details
A	GLU189
J	GLU189
B	GLU189
C	GLU189
D	GLU189
E	GLU189
F	GLU189
G	GLU189
H	GLU189
I	GLU189

site_id	SWS_FT_FI2
Number of Residues	40
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00156

Chain	Residue	Details
A	ASP53
C	ASP92
C	LYS120
C	GLU122
D	ASP53
D	ASP92
D	LYS120
D	GLU122
E	ASP53
E	ASP92
E	LYS120
A	ASP92
E	GLU122
F	ASP53
F	ASP92
F	LYS120
F	GLU122
G	ASP53
G	ASP92
G	LYS120
G	GLU122
H	ASP53
A	LYS120
H	ASP92
H	LYS120
H	GLU122
I	ASP53
I	ASP92
I	LYS120
I	GLU122
J	ASP53
J	ASP92
J	LYS120
A	GLU122
J	GLU122
B	ASP53
B	ASP92
B	LYS120
B	GLU122
C	ASP53

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