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2KI7

The solution structure of RPP29-RPP21 complex from Pyrococcus furiosus

Functional Information from GO Data
ChainGOidnamespacecontents
A0000172cellular_componentribonuclease MRP complex
A0001682biological_processtRNA 5'-leader removal
A0003723molecular_functionRNA binding
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0004526molecular_functionribonuclease P activity
A0005737cellular_componentcytoplasm
A0006364biological_processrRNA processing
A0006396biological_processRNA processing
A0008033biological_processtRNA processing
A0016787molecular_functionhydrolase activity
A0030677cellular_componentribonuclease P complex
A0033204molecular_functionribonuclease P RNA binding
B0001682biological_processtRNA 5'-leader removal
B0004518molecular_functionnuclease activity
B0004519molecular_functionendonuclease activity
B0004526molecular_functionribonuclease P activity
B0005737cellular_componentcytoplasm
B0006396biological_processRNA processing
B0008033biological_processtRNA processing
B0008270molecular_functionzinc ion binding
B0016787molecular_functionhydrolase activity
B0030677cellular_componentribonuclease P complex
B0046872molecular_functionmetal ion binding
B1902555cellular_componentendoribonuclease complex
B1990904cellular_componentribonucleoprotein complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 124
ChainResidue
BCYS63
BCYS66
BCYS92
BCYS95

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00757","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18922021","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19733182","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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