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9IP2

Cryo-EM structure of the RNA-dependent RNA polymerase complex from Marburg virus

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001172biological_processRNA-templated transcription
A0003824molecular_functioncatalytic activity
A0003924molecular_functionGTPase activity
A0003968molecular_functionRNA-directed RNA polymerase activity
A0004482molecular_functionmRNA 5'-cap (guanine-N7-)-methyltransferase activity
A0005524molecular_functionATP binding
A0006370biological_process7-methylguanosine mRNA capping
A0006397biological_processmRNA processing
A0008168molecular_functionmethyltransferase activity
A0008643biological_processcarbohydrate transport
A0015144molecular_functioncarbohydrate transmembrane transporter activity
A0016740molecular_functiontransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0016787molecular_functionhydrolase activity
A0019013cellular_componentviral nucleocapsid
A0030430cellular_componenthost cell cytoplasm
A0034062molecular_function5'-3' RNA polymerase activity
A0039689biological_processnegative stranded viral RNA replication
A0039697biological_processnegative stranded viral RNA transcription
A0046872molecular_functionmetal ion binding
A0055085biological_processtransmembrane transport
A0106005biological_processRNA 5'-cap (guanine-N7)-methylation
B0019013cellular_componentviral nucleocapsid
B0030430cellular_componenthost cell cytoplasm
B0055085biological_processtransmembrane transport
C0019013cellular_componentviral nucleocapsid
C0030430cellular_componenthost cell cytoplasm
C0055085biological_processtransmembrane transport
D0019013cellular_componentviral nucleocapsid
D0030430cellular_componenthost cell cytoplasm
D0055085biological_processtransmembrane transport
E0019013cellular_componentviral nucleocapsid
E0030430cellular_componenthost cell cytoplasm
E0055085biological_processtransmembrane transport
Functional Information from PROSITE/UniProt
site_idPS01037
Number of Residues18
DetailsSBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN
ChainResidueDetails
APRO2489-ASN2506
BPRO-279-ASN-262

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues184
DetailsDomain: {"description":"RdRp catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU00539","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"40164610","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"40164610","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"9IP2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"9IP4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Interaction with VP35","evidences":[{"source":"PubMed","id":"40164610","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues125
DetailsDomain: {"description":"VP35 IID","evidences":[{"source":"PROSITE-ProRule","id":"PRU01071","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsSite: {"description":"Interaction with L polymerase","evidences":[{"source":"PubMed","id":"40164610","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

251422

PDB entries from 2026-04-01

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