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5DIZ

Crystal Structure of nuclear proteinaceous RNase P 2 (PRORP2) from A. thaliana

Functional Information from GO Data
ChainGOidnamespacecontents
A0001682biological_processtRNA 5'-leader removal
A0004518molecular_functionnuclease activity
A0004526molecular_functionribonuclease P activity
A0005634cellular_componentnucleus
A0006397biological_processmRNA processing
A0008033biological_processtRNA processing
A0043144biological_processsno(s)RNA processing
A0043231cellular_componentintracellular membrane-bounded organelle
A0046872molecular_functionmetal ion binding
B0001682biological_processtRNA 5'-leader removal
B0004518molecular_functionnuclease activity
B0004526molecular_functionribonuclease P activity
B0005634cellular_componentnucleus
B0006397biological_processmRNA processing
B0008033biological_processtRNA processing
B0043144biological_processsno(s)RNA processing
B0043231cellular_componentintracellular membrane-bounded organelle
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 1001
ChainResidue
ACYS281
ACYS284
AHIS494
ACYS511

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN B 1001
ChainResidue
BCYS281
BCYS284
BHIS494
BCYS511

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:26655022, ECO:0007744|PDB:5DIZ
ChainResidueDetails
BHIS494
BCYS511
AHIS494
ACYS511
BCYS281
BCYS284
ACYS281
ACYS284

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305|PubMed:26655022
ChainResidueDetails
BASP343
BASP421
BASP422
BASP440
AASP422
AASP440
AASP343
AASP421

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PDB entries from 2024-05-15

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