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7C4H

Crystal structure of BCP1 from Saccharomyces Cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0000055biological_processribosomal large subunit export from nucleus
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006457biological_processprotein folding
A0006611biological_processprotein export from nucleus
A0015031biological_processprotein transport
A0044183molecular_functionprotein folding chaperone
B0000055biological_processribosomal large subunit export from nucleus
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0006457biological_processprotein folding
B0006611biological_processprotein export from nucleus
B0015031biological_processprotein transport
B0044183molecular_functionprotein folding chaperone
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue CA A 301
ChainResidue
ATRP283
BTRP283
BHOH376

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ATHR205
BTHR205

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198
ChainResidueDetails
ATHR209
BTHR209

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PDB entries from 2024-07-24

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