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6KWX

cryo-EM structure of human PA200

Functional Information from GO Data
ChainGOidnamespacecontents
A0000502cellular_componentproteasome complex
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006281biological_processDNA repair
A0006974biological_processDNA damage response
A0007283biological_processspermatogenesis
A0010499biological_processproteasomal ubiquitin-independent protein catabolic process
A0016504molecular_functionpeptidase activator activity
A0016607cellular_componentnuclear speck
A0030154biological_processcell differentiation
A0035092biological_processsperm DNA condensation
A0070577molecular_functionlysine-acetylated histone binding
A0070628molecular_functionproteasome binding
A1990111cellular_componentspermatoproteasome complex
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue K0W A 1901
ChainResidue
ALYS30
AARG943
ATYR34
AARG84
ALYS128
ALYS129
ATRP915
ALYS922
AARG928
ALYS933

site_idAC2
Number of Residues14
Detailsbinding site for residue IHP A 1902
ChainResidue
ALYS156
ALYS1213
ALYS1216
AHIS1219
ALYS1221
ALYS1271
ATYR1286
ALYS1346
AARG1350
AARG1388
ALYS1391
AHIS1392
ASER1434
AARG1435

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER1121

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER1614
ASER1746

225399

PDB entries from 2024-09-25

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