Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5UAU

Structure of human PYCR-1 complexed with proline

Functional Information from GO Data
ChainGOidnamespacecontents
A0004735molecular_functionpyrroline-5-carboxylate reductase activity
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0008652biological_processamino acid biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0034599biological_processcellular response to oxidative stress
A0042802molecular_functionidentical protein binding
A0051881biological_processregulation of mitochondrial membrane potential
A0055129biological_processL-proline biosynthetic process
A1902792cellular_componentpyrroline-5-carboxylate reductase complex
A1903377biological_processnegative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway
B0004735molecular_functionpyrroline-5-carboxylate reductase activity
B0005515molecular_functionprotein binding
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0008652biological_processamino acid biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0034599biological_processcellular response to oxidative stress
B0042802molecular_functionidentical protein binding
B0051881biological_processregulation of mitochondrial membrane potential
B0055129biological_processL-proline biosynthetic process
B1902792cellular_componentpyrroline-5-carboxylate reductase complex
B1903377biological_processnegative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway
C0004735molecular_functionpyrroline-5-carboxylate reductase activity
C0005515molecular_functionprotein binding
C0005739cellular_componentmitochondrion
C0005759cellular_componentmitochondrial matrix
C0008652biological_processamino acid biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0034599biological_processcellular response to oxidative stress
C0042802molecular_functionidentical protein binding
C0051881biological_processregulation of mitochondrial membrane potential
C0055129biological_processL-proline biosynthetic process
C1902792cellular_componentpyrroline-5-carboxylate reductase complex
C1903377biological_processnegative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway
D0004735molecular_functionpyrroline-5-carboxylate reductase activity
D0005515molecular_functionprotein binding
D0005739cellular_componentmitochondrion
D0005759cellular_componentmitochondrial matrix
D0008652biological_processamino acid biosynthetic process
D0016491molecular_functionoxidoreductase activity
D0034599biological_processcellular response to oxidative stress
D0042802molecular_functionidentical protein binding
D0051881biological_processregulation of mitochondrial membrane potential
D0055129biological_processL-proline biosynthetic process
D1902792cellular_componentpyrroline-5-carboxylate reductase complex
D1903377biological_processnegative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway
E0004735molecular_functionpyrroline-5-carboxylate reductase activity
E0005515molecular_functionprotein binding
E0005739cellular_componentmitochondrion
E0005759cellular_componentmitochondrial matrix
E0008652biological_processamino acid biosynthetic process
E0016491molecular_functionoxidoreductase activity
E0034599biological_processcellular response to oxidative stress
E0042802molecular_functionidentical protein binding
E0051881biological_processregulation of mitochondrial membrane potential
E0055129biological_processL-proline biosynthetic process
E1902792cellular_componentpyrroline-5-carboxylate reductase complex
E1903377biological_processnegative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue PRO A 401
ChainResidue
AVAL231
ASER233
AGLY236
AALA237
ATHR238
AHOH525
BTHR171
BGLY175

site_idAC2
Number of Residues6
Detailsbinding site for residue PRO A 402
ChainResidue
ATHR137
AGLU163
AGLU164
AHOH502
AHOH541
AALA136

site_idAC3
Number of Residues9
Detailsbinding site for residue PRO B 401
ChainResidue
ATHR171
AGLY175
BVAL231
BSER233
BGLY236
BALA237
BTHR238
BHOH517
BHOH541

site_idAC4
Number of Residues4
Detailsbinding site for residue PRO B 402
ChainResidue
BTHR137
BGLU163
BGLU164
BHOH513

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 B 403
ChainResidue
BGLY9
BGLN10
BLEU11
BALA69

site_idAC6
Number of Residues7
Detailsbinding site for residue PRO C 401
ChainResidue
CVAL231
CSER233
CGLY236
CALA237
CTHR238
CHOH521
DTHR171

site_idAC7
Number of Residues6
Detailsbinding site for residue PRO C 402
ChainResidue
CTHR137
CGLU163
CGLU164
CHOH501
CHOH505
CHOH548

site_idAC8
Number of Residues3
Detailsbinding site for residue SO4 C 403
ChainResidue
CGLY9
CGLN10
CLEU11

site_idAC9
Number of Residues8
Detailsbinding site for residue PRO D 401
ChainResidue
CTHR171
CGLY175
DVAL231
DSER233
DGLY236
DALA237
DTHR238
DHOH523

site_idAD1
Number of Residues4
Detailsbinding site for residue PRO D 402
ChainResidue
DTHR137
DGLU163
DGLU164
DHOH507

site_idAD2
Number of Residues3
Detailsbinding site for residue SO4 D 403
ChainResidue
DGLY9
DGLN10
DLEU11

site_idAD3
Number of Residues8
Detailsbinding site for residue PRO E 401
ChainResidue
ETHR171
EGLY175
EVAL231
ESER233
EGLY236
EALA237
ETHR238
EHOH526

site_idAD4
Number of Residues5
Detailsbinding site for residue PRO E 402
ChainResidue
ETHR137
EGLU163
EGLU164
EHOH502
EHOH538

site_idAD5
Number of Residues3
Detailsbinding site for residue SO4 E 403
ChainResidue
EGLY9
EGLN10
ELEU11

Functional Information from PROSITE/UniProt
site_idPS00521
Number of Residues23
DetailsP5CR Delta 1-pyrroline-5-carboxylate reductase signature. Pgq.LkdnVSSpGGaTihALhvLE
ChainResidueDetails
APRO224-GLU246

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues50
DetailsBinding 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)"]}}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues30
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28258219","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5UAT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5UAV","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28258219","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5UAT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28258219","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5UAV","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues15
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28258219","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5UAU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues5
DetailsModified 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"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

PDB statisticsPDBj update infoContact PDBjnumon