Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6XP0

Structure of human PYCR1 complexed with N-formyl L-proline

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004735	molecular_function	pyrroline-5-carboxylate reductase activity
A	0005515	molecular_function	protein binding
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0006561	biological_process	proline biosynthetic process
A	0008652	biological_process	amino acid biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0034599	biological_process	cellular response to oxidative stress
A	0042802	molecular_function	identical protein binding
A	0051881	biological_process	regulation of mitochondrial membrane potential
A	0055129	biological_process	L-proline biosynthetic process
A	1903377	biological_process	negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway
B	0004735	molecular_function	pyrroline-5-carboxylate reductase activity
B	0005515	molecular_function	protein binding
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0006561	biological_process	proline biosynthetic process
B	0008652	biological_process	amino acid biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0034599	biological_process	cellular response to oxidative stress
B	0042802	molecular_function	identical protein binding
B	0051881	biological_process	regulation of mitochondrial membrane potential
B	0055129	biological_process	L-proline biosynthetic process
B	1903377	biological_process	negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway
C	0004735	molecular_function	pyrroline-5-carboxylate reductase activity
C	0005515	molecular_function	protein binding
C	0005739	cellular_component	mitochondrion
C	0005759	cellular_component	mitochondrial matrix
C	0006561	biological_process	proline biosynthetic process
C	0008652	biological_process	amino acid biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
C	0034599	biological_process	cellular response to oxidative stress
C	0042802	molecular_function	identical protein binding
C	0051881	biological_process	regulation of mitochondrial membrane potential
C	0055129	biological_process	L-proline biosynthetic process
C	1903377	biological_process	negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway
D	0004735	molecular_function	pyrroline-5-carboxylate reductase activity
D	0005515	molecular_function	protein binding
D	0005739	cellular_component	mitochondrion
D	0005759	cellular_component	mitochondrial matrix
D	0006561	biological_process	proline biosynthetic process
D	0008652	biological_process	amino acid biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
D	0034599	biological_process	cellular response to oxidative stress
D	0042802	molecular_function	identical protein binding
D	0051881	biological_process	regulation of mitochondrial membrane potential
D	0055129	biological_process	L-proline biosynthetic process
D	1903377	biological_process	negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway
E	0004735	molecular_function	pyrroline-5-carboxylate reductase activity
E	0005515	molecular_function	protein binding
E	0005739	cellular_component	mitochondrion
E	0005759	cellular_component	mitochondrial matrix
E	0006561	biological_process	proline biosynthetic process
E	0008652	biological_process	amino acid biosynthetic process
E	0016491	molecular_function	oxidoreductase activity
E	0034599	biological_process	cellular response to oxidative stress
E	0042802	molecular_function	identical protein binding
E	0051881	biological_process	regulation of mitochondrial membrane potential
E	0055129	biological_process	L-proline biosynthetic process
E	1903377	biological_process	negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	binding site for residue FPK A 401

Chain	Residue
A	VAL231
A	SER233
A	GLY236
A	ALA237
A	THR238
A	HOH515
A	HOH522
B	THR171
B	GLY175

site_id	AC2
Number of Residues	10
Details	binding site for residue FPK B 401

Chain	Residue
A	ALA97
A	THR171
A	GLY175
B	VAL231
B	SER233
B	GLY236
B	ALA237
B	THR238
B	HOH506
B	HOH529

site_id	AC3
Number of Residues	8
Details	binding site for residue FPK C 401

Chain	Residue
C	VAL231
C	SER233
C	GLY236
C	ALA237
C	THR238
C	HOH526
D	THR171
D	GLY175

site_id	AC4
Number of Residues	8
Details	binding site for residue FPK D 501

Chain	Residue
C	THR171
C	GLY175
D	VAL231
D	SER233
D	GLY236
D	ALA237
D	THR238
D	HOH624

site_id	AC5
Number of Residues	9
Details	binding site for residue FPK E 401

Chain	Residue
E	ALA97
E	THR171
E	GLY175
E	VAL231
E	SER233
E	GLY236
E	ALA237
E	THR238
E	HOH533

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PRO224-GLU246

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	15
Details	BINDING: BINDING => ECO:0000269\|Ref.19

Chain	Residue	Details
A	ILE6
D	ILE6
D	ALA69
D	CYS95
E	ILE6
E	ALA69
E	CYS95
A	ALA69
A	CYS95
B	ILE6
B	ALA69
B	CYS95
C	ILE6
C	ALA69
C	CYS95

site_id	SWS_FT_FI2
Number of Residues	30
Details	BINDING: BINDING => ECO:0000269\|PubMed:28258219, ECO:0007744\|PDB:5UAT, ECO:0007744\|PDB:5UAV

Chain	Residue	Details
A	ALA8
B	ASP36
B	VAL70
B	ALA97
C	ALA8
C	GLN10
C	LEU11
C	ASP36
C	VAL70
C	ALA97
D	ALA8
A	GLN10
D	GLN10
D	LEU11
D	ASP36
D	VAL70
D	ALA97
E	ALA8
E	GLN10
E	LEU11
E	ASP36
E	VAL70
A	LEU11
E	ALA97
A	ASP36
A	VAL70
A	ALA97
B	ALA8
B	GLN10
B	LEU11

site_id	SWS_FT_FI3
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269\|PubMed:28258219, ECO:0007744\|PDB:5UAT

Chain	Residue	Details
A	SER34
E	ASN230
A	ASN230
B	SER34
B	ASN230
C	SER34
C	ASN230
D	SER34
D	ASN230
E	SER34

site_id	SWS_FT_FI4
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269\|PubMed:28258219, ECO:0007744\|PDB:5UAV

Chain	Residue	Details
A	ASN56
E	LYS71
A	LYS71
B	ASN56
B	LYS71
C	ASN56
C	LYS71
D	ASN56
D	LYS71
E	ASN56

site_id	SWS_FT_FI5
Number of Residues	15
Details	BINDING: BINDING => ECO:0000269\|PubMed:28258219, ECO:0007744\|PDB:5UAU

Chain	Residue	Details
A	GLU164
D	GLU164
D	ALA237
D	THR238
E	GLU164
E	ALA237
E	THR238
A	ALA237
A	THR238
B	GLU164
B	ALA237
B	THR238
C	GLU164
C	ALA237
C	THR238

site_id	SWS_FT_FI6
Number of Residues	5
Details	MOD_RES: N-acetylserine => ECO:0000269\|Ref.8, ECO:0000269\|Ref.9, ECO:0007744\|PubMed:19413330

Chain	Residue	Details
A	SER2
B	SER2
C	SER2
D	SER2
E	SER2

site_id	SWS_FT_FI7
Number of Residues	5
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER278
B	SER278
C	SER278
D	SER278
E	SER278

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