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5ZK6

Crystal structure of RimK complexed with RpsF

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006412biological_processtranslation
A0009432biological_processSOS response
A0016874molecular_functionligase activity
A0018169molecular_functionribosomal S6-glutamic acid ligase activity
A0018410biological_processC-terminal protein amino acid modification
A0036211biological_processprotein modification process
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue ADP A 1001
ChainResidue
ALYS141
ASER212
AASN213
AARG216
ALEU250
AMET259
AGLU260
AMG1002
AVAL151
AGLN177
AGLU178
ATYR179
AILE180
AARG203
APHE210
AARG211

site_idAC2
Number of Residues3
Detailsbinding site for residue MG A 1002
ChainResidue
AASN213
AGLU260
AADP1001

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues183
DetailsDomain: {"description":"ATP-grasp","evidences":[{"source":"HAMAP-Rule","id":"MF_01552","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23609986","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01552","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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