Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4H67

Crystal structure of HMP synthase Thi5 from S. cerevisiae

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003674	molecular_function	molecular_function
A	0005506	molecular_function	iron ion binding
A	0005515	molecular_function	protein binding
A	0005575	cellular_component	cellular_component
A	0009228	biological_process	thiamine biosynthetic process
A	0009229	biological_process	thiamine diphosphate biosynthetic process
A	0106344	molecular_function	4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase activity from histidine and PLP
B	0003674	molecular_function	molecular_function
B	0005506	molecular_function	iron ion binding
B	0005515	molecular_function	protein binding
B	0005575	cellular_component	cellular_component
B	0009228	biological_process	thiamine biosynthetic process
B	0009229	biological_process	thiamine diphosphate biosynthetic process
B	0106344	molecular_function	4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase activity from histidine and PLP
C	0003674	molecular_function	molecular_function
C	0005506	molecular_function	iron ion binding
C	0005515	molecular_function	protein binding
C	0005575	cellular_component	cellular_component
C	0009228	biological_process	thiamine biosynthetic process
C	0009229	biological_process	thiamine diphosphate biosynthetic process
C	0106344	molecular_function	4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase activity from histidine and PLP
D	0003674	molecular_function	molecular_function
D	0005506	molecular_function	iron ion binding
D	0005515	molecular_function	protein binding
D	0005575	cellular_component	cellular_component
D	0009228	biological_process	thiamine biosynthetic process
D	0009229	biological_process	thiamine diphosphate biosynthetic process
D	0106344	molecular_function	4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase activity from histidine and PLP
E	0003674	molecular_function	molecular_function
E	0005506	molecular_function	iron ion binding
E	0005515	molecular_function	protein binding
E	0005575	cellular_component	cellular_component
E	0009228	biological_process	thiamine biosynthetic process
E	0009229	biological_process	thiamine diphosphate biosynthetic process
E	0106344	molecular_function	4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase activity from histidine and PLP
F	0003674	molecular_function	molecular_function
F	0005506	molecular_function	iron ion binding
F	0005515	molecular_function	protein binding
F	0005575	cellular_component	cellular_component
F	0009228	biological_process	thiamine biosynthetic process
F	0009229	biological_process	thiamine diphosphate biosynthetic process
F	0106344	molecular_function	4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase activity from histidine and PLP
G	0003674	molecular_function	molecular_function
G	0005506	molecular_function	iron ion binding
G	0005515	molecular_function	protein binding
G	0005575	cellular_component	cellular_component
G	0009228	biological_process	thiamine biosynthetic process
G	0009229	biological_process	thiamine diphosphate biosynthetic process
G	0106344	molecular_function	4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase activity from histidine and PLP
H	0003674	molecular_function	molecular_function
H	0005506	molecular_function	iron ion binding
H	0005515	molecular_function	protein binding
H	0005575	cellular_component	cellular_component
H	0009228	biological_process	thiamine biosynthetic process
H	0009229	biological_process	thiamine diphosphate biosynthetic process
H	0106344	molecular_function	4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase activity from histidine and PLP

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 401

Chain	Residue
A	SER267
A	ARG335

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 402

Chain	Residue
A	HIS342
A	HIS343
A	HIS344
A	HIS345
D	LYS277

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 403

Chain	Residue
A	GLY115
A	GLU116
A	PHE117
A	GLY118
A	HIS66
A	VAL114

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PLP B 400

Chain	Residue
B	ASN11
B	LYS62
B	HIS66
B	VAL114
B	GLY115
B	GLU116
B	PHE117
B	GLY118

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 401

Chain	Residue
C	HIS344
G	THR298
G	ASN299
G	GLU300

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 C 402

Chain	Residue
C	SER267
C	ARG335

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 403

Chain	Residue
C	PRO178
C	ALA179
C	SER180
C	ARG328

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 C 404

Chain	Residue
C	HIS273
C	ASN299

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 405

Chain	Residue
C	HIS341
C	HIS343
G	LYS277

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 406

Chain	Residue
C	HIS66
C	VAL114
C	GLY115
C	GLU116
C	PHE117
C	GLY118

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 401

Chain	Residue
A	HIS345
D	HIS273
D	THR298
D	ASN299
D	GLU300

site_id	BC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 D 402

Chain	Residue
D	SER267
D	ARG335

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 403

Chain	Residue
D	HIS66
D	VAL114
D	GLY115
D	GLU116
D	PHE117
D	GLY118

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 E 401

Chain	Residue
E	HIS66
E	VAL114
E	GLY115
E	PHE117
E	GLY118

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 F 401

Chain	Residue
F	HIS66
F	VAL114
F	GLY115
F	GLU116
F	PHE117
F	GLY118

site_id	BC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 G 401

Chain	Residue
G	SER267
G	ARG335

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 G 402

Chain	Residue
G	HIS66
G	VAL114
G	GLY115
G	GLU116
G	PHE117
G	GLY118

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 H 401

Chain	Residue
H	HIS66
H	VAL114
H	GLY115
H	GLU116
H	PHE117
H	GLY118

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"evidences":[{"source":"PubMed","id":"23048037","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"23048037","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"23048037","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	16
Details	Motif: {"description":"CCCFC; essential for catalytic activity, may be the site of iron coordination","evidences":[{"source":"PubMed","id":"23048037","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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