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4D4O

Crystal Structure of the Kti11 Kti13 heterodimer Spacegroup P64

Functional Information from GO Data
ChainGOidnamespacecontents
A0002098biological_processtRNA wobble uridine modification
A0002926biological_processtRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation
A0003674molecular_functionmolecular_function
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006511biological_processubiquitin-dependent protein catabolic process
A0008033biological_processtRNA processing
A0008198molecular_functionferrous iron binding
A0008270molecular_functionzinc ion binding
A0016491molecular_functionoxidoreductase activity
A0016567biological_processprotein ubiquitination
A0016730molecular_functionoxidoreductase activity, acting on iron-sulfur proteins as donors
A0017183biological_processprotein histidyl modification to diphthamide
A0034986molecular_functioniron chaperone activity
A0046872molecular_functionmetal ion binding
A0061630molecular_functionubiquitin protein ligase activity
A0090560molecular_function2-(3-amino-3-carboxypropyl)histidine synthase activity
B0002098biological_processtRNA wobble uridine modification
B0002926biological_processtRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation
B0003674molecular_functionmolecular_function
B0005506molecular_functioniron ion binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006511biological_processubiquitin-dependent protein catabolic process
B0008033biological_processtRNA processing
B0008198molecular_functionferrous iron binding
B0008270molecular_functionzinc ion binding
B0016491molecular_functionoxidoreductase activity
B0016567biological_processprotein ubiquitination
B0016730molecular_functionoxidoreductase activity, acting on iron-sulfur proteins as donors
B0017183biological_processprotein histidyl modification to diphthamide
B0034986molecular_functioniron chaperone activity
B0046872molecular_functionmetal ion binding
B0061630molecular_functionubiquitin protein ligase activity
B0090560molecular_function2-(3-amino-3-carboxypropyl)histidine synthase activity
C0002098biological_processtRNA wobble uridine modification
C0002926biological_processtRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation
C0003674molecular_functionmolecular_function
C0005506molecular_functioniron ion binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006511biological_processubiquitin-dependent protein catabolic process
C0008033biological_processtRNA processing
C0008198molecular_functionferrous iron binding
C0008270molecular_functionzinc ion binding
C0016491molecular_functionoxidoreductase activity
C0016567biological_processprotein ubiquitination
C0016730molecular_functionoxidoreductase activity, acting on iron-sulfur proteins as donors
C0017183biological_processprotein histidyl modification to diphthamide
C0034986molecular_functioniron chaperone activity
C0046872molecular_functionmetal ion binding
C0061630molecular_functionubiquitin protein ligase activity
C0090560molecular_function2-(3-amino-3-carboxypropyl)histidine synthase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE A 501
ChainResidue
ACYS368
ACYS370
ACYS390
ACYS393

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE C 501
ChainResidue
CCYS368
CCYS370
CCYS390
CCYS393

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 1420
ChainResidue
AGLN120
AARG107

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 1336
ChainResidue
BARG107
BGLN120
BHIS122

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 1337
ChainResidue
BARG220
BASN236
BARG238

Functional Information from PROSITE/UniProt
site_idPS00626
Number of Residues11
DetailsRCC1_2 Regulator of chromosome condensation (RCC1) signature 2. IACGgNHSVML
ChainResidueDetails
AILE41-LEU51

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues104
DetailsRepeat: {"description":"RCC1 1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues98
DetailsRepeat: {"description":"RCC1 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues102
DetailsRepeat: {"description":"RCC1 3"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues94
DetailsRepeat: {"description":"RCC1 4"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues112
DetailsDomain: {"description":"DPH-type MB","evidences":[{"source":"PROSITE-ProRule","id":"PRU00456","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25543256","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25604895","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4D4O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4D4P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4X33","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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