Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3CM6

Crystal structure of cell-death related nuclease 4 (CRN-4) bound with Er

Functional Information from GO Data
ChainGOidnamespacecontents
A0000175molecular_function3'-5'-RNA exonuclease activity
A0000467biological_processexonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
A0003676molecular_functionnucleic acid binding
A0003697molecular_functionsingle-stranded DNA binding
A0004520molecular_functionDNA endonuclease activity
A0004527molecular_functionexonuclease activity
A0004536molecular_functionDNA nuclease activity
A0004540molecular_functionRNA nuclease activity
A0005737cellular_componentcytoplasm
A0006308biological_processDNA catabolic process
A0006309biological_processapoptotic DNA fragmentation
A0006401biological_processRNA catabolic process
A0006915biological_processapoptotic process
A0008408molecular_function3'-5' exonuclease activity
A0046872molecular_functionmetal ion binding
B0000175molecular_function3'-5'-RNA exonuclease activity
B0000467biological_processexonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
B0003676molecular_functionnucleic acid binding
B0003697molecular_functionsingle-stranded DNA binding
B0004520molecular_functionDNA endonuclease activity
B0004527molecular_functionexonuclease activity
B0004536molecular_functionDNA nuclease activity
B0004540molecular_functionRNA nuclease activity
B0005737cellular_componentcytoplasm
B0006308biological_processDNA catabolic process
B0006309biological_processapoptotic DNA fragmentation
B0006401biological_processRNA catabolic process
B0006915biological_processapoptotic process
B0008408molecular_function3'-5' exonuclease activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 299
ChainResidue
ACYS210
ACYS260
ACYS263
ACYS270

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ER3 A 300
ChainResidue
AASP15
APHE16
AGLU17
AASP184

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 299
ChainResidue
BCYS260
BCYS263
BCYS270
BCYS210

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ER3 B 300
ChainResidue
BASP15
BGLU17
BASP184

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:27529560, ECO:0007744|PDB:5DK5
ChainResidueDetails
AASP15
AGLU17
AASP184
BASP15
BGLU17
BASP184

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:18981218, ECO:0000269|PubMed:27529560, ECO:0007744|PDB:3CG7, ECO:0007744|PDB:3CM5, ECO:0007744|PDB:3CM6, ECO:0007744|PDB:5DK5
ChainResidueDetails
ACYS210
ACYS260
ACYS263
ACYS270
BCYS210
BCYS260
BCYS263
BCYS270

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon