Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5UAV

Structure of human PYCR-1 complexed with NADPH and L-tetrahydrofuroic acid

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	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	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	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	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	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	30
Details	binding site for residue NDP A 401

Chain	Residue
A	GLY7
A	ASN56
A	ALA69
A	VAL70
A	LYS71
A	PRO72
A	ILE78
A	CYS95
A	ALA96
A	ALA97
A	MET121
A	ALA8
A	THR122
A	THR124
A	HOH518
A	HOH534
A	HOH538
A	HOH556
A	HOH562
B	ASN230
B	VAL231
B	TFB402
A	GLY9
B	HOH581
A	GLN10
A	LEU11
A	SER33
A	SER34
A	PRO35
A	ASP36

site_id	AC2
Number of Residues	8
Details	binding site for residue TFB A 402

Chain	Residue
A	GLY236
A	ALA237
A	THR238
A	HOH501
A	HOH508
A	HOH539
B	GLY175
B	NDP401

site_id	AC3
Number of Residues	31
Details	binding site for residue NDP B 401

Chain	Residue
A	TFB402
A	HOH508
A	HOH571
B	GLY7
B	ALA8
B	GLY9
B	GLN10
B	LEU11
B	SER33
B	SER34
B	PRO35
B	ASP36
B	ASN56
B	ALA69
B	VAL70
B	LYS71
B	PRO72
B	ILE78
B	CYS95
B	ALA96
B	ALA97
B	MET121
B	THR122
B	THR124
B	HOH512
B	HOH513
B	HOH514
B	HOH554
B	HOH557
B	HOH564
B	HOH575

site_id	AC4
Number of Residues	8
Details	binding site for residue TFB B 402

Chain	Residue
A	GLY175
A	NDP401
B	VAL231
B	SER233
B	ALA237
B	THR238
B	HOH503
B	HOH533

site_id	AC5
Number of Residues	36
Details	binding site for residue NDP C 401

Chain	Residue
C	HOH508
C	HOH531
C	HOH532
C	HOH535
C	HOH540
C	HOH553
C	HOH564
C	HOH566
C	HOH572
C	HOH573
C	HOH592
C	HOH618
D	VAL231
D	TFB402
C	GLY7
C	ALA8
C	GLY9
C	GLN10
C	LEU11
C	SER34
C	PRO35
C	ASP36
C	MET37
C	ASN56
C	ALA69
C	VAL70
C	LYS71
C	PRO72
C	ILE78
C	CYS95
C	ALA96
C	ALA97
C	MET121
C	THR122
C	THR124
C	HOH503

site_id	AC6
Number of Residues	8
Details	binding site for residue TFB C 402

Chain	Residue
C	SER233
C	ALA237
C	THR238
C	HOH515
D	THR171
D	GLY175
D	NDP401
D	HOH541

site_id	AC7
Number of Residues	4
Details	binding site for residue PEG C 403

Chain	Residue
B	ASP64
B	ARG89
C	LEU39
C	HOH600

site_id	AC8
Number of Residues	31
Details	binding site for residue NDP D 401

Chain	Residue
C	VAL231
C	TFB402
C	HOH565
D	GLY7
D	ALA8
D	GLY9
D	GLN10
D	LEU11
D	SER33
D	SER34
D	PRO35
D	ASP36
D	ASN56
D	ALA69
D	VAL70
D	LYS71
D	PRO72
D	ILE78
D	CYS95
D	ALA96
D	ALA97
D	MET121
D	THR122
D	THR124
D	HOH515
D	HOH520
D	HOH541
D	HOH550
D	HOH566
D	HOH572
D	HOH600

site_id	AC9
Number of Residues	10
Details	binding site for residue TFB D 402

Chain	Residue
C	THR171
C	GLY175
C	NDP401
C	HOH508
D	SER233
D	GLY236
D	ALA237
D	THR238
D	HOH502
D	HOH526

site_id	AD1
Number of Residues	33
Details	binding site for residue NDP E 401

Chain	Residue
E	GLY7
E	ALA8
E	GLY9
E	GLN10
E	LEU11
E	SER34
E	PRO35
E	ASP36
E	MET37
E	ASN56
E	ALA69
E	VAL70
E	LYS71
E	PRO72
E	ILE78
E	CYS95
E	ALA96
E	ALA97
E	MET121
E	THR122
E	THR124
E	ASN230
E	VAL231
E	TFB402
E	HOH515
E	HOH522
E	HOH530
E	HOH538
E	HOH553
E	HOH555
E	HOH558
E	HOH579
E	HOH588

site_id	AD2
Number of Residues	9
Details	binding site for residue TFB E 402

Chain	Residue
E	THR171
E	GLY175
E	VAL231
E	SER233
E	ALA237
E	THR238
E	NDP401
E	HOH515
E	HOH550

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	25
Details	BINDING: BINDING => ECO:0000269\|Ref.18

Chain	Residue	Details
A	ILE6
B	CYS95
C	ILE6
C	SER34
C	ASN56
C	ALA69
C	CYS95
D	ILE6
D	SER34
D	ASN56
D	ALA69
A	SER34
D	CYS95
E	ILE6
E	SER34
E	ASN56
E	ALA69
E	CYS95
A	ASN56
A	ALA69
A	CYS95
B	ILE6
B	SER34
B	ASN56
B	ALA69

site_id	SWS_FT_FI2
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_FI3
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)