1UMD

branched-chain 2-oxo acid dehydrogenase (E1) from Thermus thermophilus HB8 with 4-methyl-2-oxopentanoate as an intermediate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003863	molecular_function	branched-chain 2-oxo acid dehydrogenase activity
A	0005515	molecular_function	protein binding
A	0009083	biological_process	branched-chain amino acid catabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0016624	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
A	0046872	molecular_function	metal ion binding
B	0003863	molecular_function	branched-chain 2-oxo acid dehydrogenase activity
B	0005515	molecular_function	protein binding
B	0016491	molecular_function	oxidoreductase activity
C	0003863	molecular_function	branched-chain 2-oxo acid dehydrogenase activity
C	0005515	molecular_function	protein binding
C	0009083	biological_process	branched-chain amino acid catabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0016624	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
C	0046872	molecular_function	metal ion binding
D	0003863	molecular_function	branched-chain 2-oxo acid dehydrogenase activity
D	0005515	molecular_function	protein binding
D	0016491	molecular_function	oxidoreductase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 1401

Chain	Residue
A	ASP175
A	ASN204
A	TYR206
A	TPP1402
A	HOH1435

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 2401

Chain	Residue
C	HOH2425
C	ASP175
C	ASN204
C	TYR206
C	TPP2402

---

site_id	AC3
Number of Residues	26
Details	BINDING SITE FOR RESIDUE TPP A 1402

Chain	Residue
A	TYR94
A	TYR95
A	ARG96
A	SER144
A	PRO145
A	ILE146
A	GLY174
A	ASP175
A	GLY176
A	ALA177
A	GLU180
A	ASN204
A	TYR206
A	ALA207
A	ILE208
A	HIS273
A	MG1401
A	COI1403
A	HOH1413
A	HOH1434
A	HOH1435
D	GLU29
D	LEU58
D	GLU60
D	GLN82
D	TYR86

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE COI A 1403

Chain	Residue
A	PHE66
A	SER144
A	TPP1402
D	TYR86
D	HIS129

---

site_id	AC5
Number of Residues	26
Details	BINDING SITE FOR RESIDUE TPP C 2402

Chain	Residue
B	GLU29
B	LEU58
B	GLU60
B	GLN82
B	TYR86
C	TYR94
C	TYR95
C	ARG96
C	SER144
C	PRO145
C	ILE146
C	GLY174
C	ASP175
C	GLY176
C	ALA177
C	GLU180
C	ASN204
C	TYR206
C	ALA207
C	ILE208
C	HIS273
C	MG2401
C	COI2403
C	HOH2422
C	HOH2425
C	HOH2439

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE COI C 2403

Chain	Residue
B	TYR86
B	HIS129
C	PHE66
C	SER144
C	TPP2402

---

Functional Information from PROSITE/UniProt

site_id	PS00014
Number of Residues	4
Details	ER_TARGET Endoplasmic reticulum targeting sequence. KEEL

Chain	Residue	Details
A	LYS364-LEU367

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	52
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15033367","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	16
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
C	HIS273
B	GLU60
B	HIS129

---

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1dtw

Chain	Residue	Details
A	HIS273
D	GLU60
D	HIS129

---