6XP2

Structure of human PYCR1 complexed with L-thiazolidine-4-carboxylate

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	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	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	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	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	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	7
Details	binding site for residue PRS A 401

Chain	Residue
A	VAL231
A	SER233
A	ALA237
A	THR238
A	HOH502
B	THR171
B	GLY175

---

site_id	AC2
Number of Residues	6
Details	binding site for residue SO4 B 401

Chain	Residue
B	ALA237
B	THR238
B	HOH507
B	HOH512
B	VAL231
B	SER233

---

site_id	AC3
Number of Residues	6
Details	binding site for residue SO4 C 401

Chain	Residue
C	VAL231
C	SER233
C	ALA237
C	THR238
C	HOH514
C	HOH517

---

site_id	AC4
Number of Residues	7
Details	binding site for residue SO4 D 401

Chain	Residue
D	VAL231
D	SER233
D	GLY236
D	ALA237
D	THR238
D	HOH515
D	HOH517

---

site_id	AC5
Number of Residues	6
Details	binding site for residue PRS E 401

Chain	Residue
E	GLY175
E	VAL231
E	SER233
E	ALA237
E	THR238
E	HOH502

---

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	28
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_FI2
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_FI3
Number of Residues	45
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_FI4
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_FI5
Number of Residues	9
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_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

---