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1YOP

The solution structure of Kti11p

Functional Information from GO Data
ChainGOidnamespacecontents
A0002098biological_processtRNA wobble uridine modification
A0002926biological_processtRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008033biological_processtRNA processing
A0008198molecular_functionferrous iron binding
A0008270molecular_functionzinc ion binding
A0016491molecular_functionoxidoreductase activity
A0016730molecular_functionoxidoreductase activity, acting on iron-sulfur proteins as donors
A0017183biological_processprotein histidyl modification to diphthamide
A0034986molecular_functioniron chaperone activity
A0046872molecular_functionmetal ion binding
A0090560molecular_function2-(3-amino-3-carboxypropyl)histidine synthase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 84
ChainResidue
ACYS26
ACYS28
ACYS48
ACYS51

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:25543256, ECO:0000269|PubMed:25604895, ECO:0007744|PDB:4D4O, ECO:0007744|PDB:4D4P, ECO:0007744|PDB:4X33
ChainResidueDetails
ACYS26
ACYS28
ACYS48
ACYS51

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PDB entries from 2024-07-17

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