Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5BSH

Crystal structure of Medicago truncatula (delta)1-Pyrroline-5-Carboxylate Reductase (MtP5CR) in complex with L-Proline

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004735	molecular_function	pyrroline-5-carboxylate reductase activity
A	0006561	biological_process	proline biosynthetic process
A	0008652	biological_process	amino acid biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0055129	biological_process	L-proline biosynthetic process
B	0000166	molecular_function	nucleotide binding
B	0004735	molecular_function	pyrroline-5-carboxylate reductase activity
B	0006561	biological_process	proline biosynthetic process
B	0008652	biological_process	amino acid biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0055129	biological_process	L-proline biosynthetic process
C	0000166	molecular_function	nucleotide binding
C	0004735	molecular_function	pyrroline-5-carboxylate reductase activity
C	0006561	biological_process	proline biosynthetic process
C	0008652	biological_process	amino acid biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
C	0055129	biological_process	L-proline biosynthetic process
D	0000166	molecular_function	nucleotide binding
D	0004735	molecular_function	pyrroline-5-carboxylate reductase activity
D	0006561	biological_process	proline biosynthetic process
D	0008652	biological_process	amino acid biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
D	0055129	biological_process	L-proline biosynthetic process
E	0000166	molecular_function	nucleotide binding
E	0004735	molecular_function	pyrroline-5-carboxylate reductase activity
E	0006561	biological_process	proline biosynthetic process
E	0008652	biological_process	amino acid biosynthetic process
E	0016491	molecular_function	oxidoreductase activity
E	0055129	biological_process	L-proline biosynthetic process
F	0000166	molecular_function	nucleotide binding
F	0004735	molecular_function	pyrroline-5-carboxylate reductase activity
F	0006561	biological_process	proline biosynthetic process
F	0008652	biological_process	amino acid biosynthetic process
F	0016491	molecular_function	oxidoreductase activity
F	0055129	biological_process	L-proline biosynthetic process
G	0000166	molecular_function	nucleotide binding
G	0004735	molecular_function	pyrroline-5-carboxylate reductase activity
G	0006561	biological_process	proline biosynthetic process
G	0008652	biological_process	amino acid biosynthetic process
G	0016491	molecular_function	oxidoreductase activity
G	0055129	biological_process	L-proline biosynthetic process
H	0000166	molecular_function	nucleotide binding
H	0004735	molecular_function	pyrroline-5-carboxylate reductase activity
H	0006561	biological_process	proline biosynthetic process
H	0008652	biological_process	amino acid biosynthetic process
H	0016491	molecular_function	oxidoreductase activity
H	0055129	biological_process	L-proline biosynthetic process
I	0000166	molecular_function	nucleotide binding
I	0004735	molecular_function	pyrroline-5-carboxylate reductase activity
I	0006561	biological_process	proline biosynthetic process
I	0008652	biological_process	amino acid biosynthetic process
I	0016491	molecular_function	oxidoreductase activity
I	0055129	biological_process	L-proline biosynthetic process
J	0000166	molecular_function	nucleotide binding
J	0004735	molecular_function	pyrroline-5-carboxylate reductase activity
J	0006561	biological_process	proline biosynthetic process
J	0008652	biological_process	amino acid biosynthetic process
J	0016491	molecular_function	oxidoreductase activity
J	0055129	biological_process	L-proline biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue PRO A 301

Chain	Residue
A	VAL236
A	SER238
A	GLY241
A	THR242
A	THR243
A	HOH421
B	GLY180

site_id	AC2
Number of Residues	7
Details	binding site for residue PRO B 301

Chain	Residue
B	SER238
B	GLY241
B	THR242
B	THR243
B	HOH419
A	GLY180
B	VAL236

site_id	AC3
Number of Residues	7
Details	binding site for residue PRO C 301

Chain	Residue
C	VAL236
C	SER238
C	GLY241
C	THR242
C	THR243
C	HOH402
D	GLY180

site_id	AC4
Number of Residues	7
Details	binding site for residue PRO D 301

Chain	Residue
C	GLY180
D	VAL236
D	SER238
D	GLY241
D	THR242
D	THR243
D	HOH405

site_id	AC5
Number of Residues	7
Details	binding site for residue PRO E 301

Chain	Residue
E	VAL236
E	SER238
E	GLY241
E	THR242
E	THR243
E	HOH417
F	GLY180

site_id	AC6
Number of Residues	7
Details	binding site for residue PRO F 301

Chain	Residue
E	GLY180
F	VAL236
F	SER238
F	GLY241
F	THR242
F	THR243
F	HOH404

site_id	AC7
Number of Residues	8
Details	binding site for residue PRO G 301

Chain	Residue
G	VAL236
G	SER238
G	GLY241
G	THR242
G	THR243
G	HOH414
H	THR176
H	GLY180

site_id	AC8
Number of Residues	7
Details	binding site for residue PRO H 301

Chain	Residue
G	GLY180
H	VAL236
H	SER238
H	GLY241
H	THR242
H	THR243
H	HOH403

site_id	AC9
Number of Residues	7
Details	binding site for residue PRO I 301

Chain	Residue
I	VAL236
I	SER238
I	GLY241
I	THR242
I	THR243
I	HOH404
J	GLY180

site_id	AD1
Number of Residues	7
Details	binding site for residue PRO J 301

Chain	Residue
I	GLY180
J	VAL236
J	SER238
J	GLY241
J	THR242
J	THR243
J	HOH406

Functional Information from PROSITE/UniProt

site_id	PS00521
Number of Residues	23
Details	P5CR Delta 1-pyrroline-5-carboxylate reductase signature. Pgq.LkddVTSpGGtTiaGVheLE

Chain	Residue	Details
A	PRO229-GLU251

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