Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2IZZ

Crystal structure of human pyrroline-5-carboxylate reductase

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	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	1902792	cellular_component	pyrroline-5-carboxylate reductase complex
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	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	1902792	cellular_component	pyrroline-5-carboxylate reductase complex
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	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	1902792	cellular_component	pyrroline-5-carboxylate reductase complex
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	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	1902792	cellular_component	pyrroline-5-carboxylate reductase complex
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	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	1902792	cellular_component	pyrroline-5-carboxylate reductase complex
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	33
Details	BINDING SITE FOR RESIDUE NAD A 350

Chain	Residue
A	ILE6
A	LEU39
A	ASN56
A	ALA69
A	VAL70
A	LYS71
A	PRO72
A	ILE78
A	CYS95
A	ALA96
A	ALA97
A	GLY7
A	MET121
A	THR122
A	THR124
A	EDO1273
A	HOH2026
A	HOH2036
A	HOH2146
A	HOH2147
A	HOH2148
A	HOH2150
A	ALA8
A	HOH2151
B	ASN230
B	VAL231
B	SER233
A	GLY9
A	GLN10
A	LEU11
A	SER33
A	SER34
A	PRO35

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A1272

Chain	Residue
A	VAL231
A	THR238
A	HOH2152
B	GLY175
B	NAD350

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A1273

Chain	Residue
A	GLY175
A	NAD350
A	HOH2153
B	VAL231
B	THR238

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A1274

Chain	Residue
A	ASN230
A	SER233
A	HOH2113
A	HOH2154
B	LYS71
B	NAD350

site_id	AC5
Number of Residues	32
Details	BINDING SITE FOR RESIDUE NAD B 350

Chain	Residue
A	ASN230
A	VAL231
A	EDO1272
A	EDO1274
A	HOH2117
B	GLY7
B	ALA8
B	GLY9
B	GLN10
B	LEU11
B	SER34
B	PRO35
B	LEU39
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	HOH2038
B	HOH2161
B	HOH2162
B	HOH2163
B	HOH2164
B	HOH2165
B	HOH2166

site_id	AC6
Number of Residues	29
Details	BINDING SITE FOR RESIDUE NAD C 350

Chain	Residue
C	THR124
C	EDO1277
C	HOH2121
C	HOH2122
C	HOH2123
C	HOH2124
C	HOH2125
C	HOH2126
D	ASN230
D	VAL231
D	EDO1272
C	ILE6
C	GLY7
C	ALA8
C	GLY9
C	GLN10
C	LEU11
C	SER34
C	PRO35
C	ASN56
C	ALA69
C	VAL70
C	LYS71
C	PRO72
C	ILE78
C	CYS95
C	ALA96
C	ALA97
C	THR122

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO C1276

Chain	Residue
C	VAL231
C	SER233
C	THR238
D	NAD350

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO C1277

Chain	Residue
C	ALA97
C	THR171
C	GLY175
C	NAD350
C	HOH2127
D	VAL231
D	THR238

site_id	AC9
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAD D 350

Chain	Residue
C	ASN230
C	VAL231
C	SER233
C	EDO1276
D	ALA8
D	GLY9
D	GLN10
D	LEU11
D	SER33
D	SER34
D	PRO35
D	LEU39
D	ASN56
D	ALA69
D	VAL70
D	LYS71
D	PRO72
D	CYS95
D	ALA96
D	ALA97
D	THR122
D	THR124
D	HOH2122
D	HOH2123
D	HOH2125
D	HOH2126

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO D1272

Chain	Residue
C	NAD350
D	ASN230
D	SER233
D	HOH2127

site_id	BC2
Number of Residues	24
Details	BINDING SITE FOR RESIDUE NAD E 350

Chain	Residue
E	GLY7
E	ALA8
E	GLY9
E	GLN10
E	LEU11
E	SER34
E	PRO35
E	LEU39
E	ASN56
E	ALA69
E	VAL70
E	LYS71
E	PRO72
E	CYS95
E	ALA96
E	ALA97
E	THR122
E	THR124
E	VAL231
E	EDO1273
E	HOH2117
E	HOH2118
E	HOH2119
E	HOH2120

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO E1273

Chain	Residue
E	LYS71
E	ASN230
E	SER233
E	NAD350

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	50
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human pyrroline-5-carboxylate reductase.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	30
Details	Binding site: {"evidences":[{"source":"PubMed","id":"28258219","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5UAT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5UAV","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"28258219","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5UAT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PubMed","id":"28258219","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5UAV","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	15
Details	Binding site: {"evidences":[{"source":"PubMed","id":"28258219","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5UAU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	5
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Zebisch A.","Kolch W."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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