5M42

Structure of Thermus thermophilus L-proline dehydrogenase lacking alpha helices A, B and C

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004657	molecular_function	proline dehydrogenase activity
A	0006562	biological_process	proline catabolic process
A	0010133	biological_process	proline catabolic process to glutamate

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	binding site for residue FMN A 2001

Chain	Residue
A	ASP133
A	ALA225
A	THR226
A	HIS227
A	LEU254
A	TYR275
A	HOH2102
A	HOH2121
A	MET134
A	VAL161
A	GLN163
A	ARG184
A	VAL186
A	LYS187
A	GLY188
A	ALA189

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000305|PubMed:18426222

Chain	Residue	Details
A	ASP133
A	ARG184

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q9RW55

Chain	Residue	Details
A	LYS99
A	ARG288

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:17344208, ECO:0000269|PubMed:18426222, ECO:0007744|PDB:2EKG, ECO:0007744|PDB:2G37

Chain	Residue	Details
A	MET134
A	GLN163
A	LYS187
A	THR226

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:17344208, ECO:0007744|PDB:2G37

Chain	Residue	Details
A	LYS201

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	SITE: Critical for catalytic activity => ECO:0000305|PubMed:18426222

Chain	Residue	Details
A	TYR275

---