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7PYV

Crystal structure of human UBA6 in complex with the ubiquitin-like modifier FAT10

Functional Information from GO Data
ChainGOidnamespacecontents
A0008641molecular_functionubiquitin-like modifier activating enzyme activity
A0036211biological_processprotein modification process
B0008641molecular_functionubiquitin-like modifier activating enzyme activity
B0036211biological_processprotein modification process
C0001650cellular_componentfibrillar center
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006508biological_processproteolysis
C0006511biological_processubiquitin-dependent protein catabolic process
C0006950biological_processresponse to stress
C0016235cellular_componentaggresome
C0016567biological_processprotein ubiquitination
C0032446biological_processprotein modification by small protein conjugation
C0034341biological_processresponse to type II interferon
C0034612biological_processresponse to tumor necrosis factor
C0043011biological_processmyeloid dendritic cell differentiation
C0043065biological_processpositive regulation of apoptotic process
C0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
C0070628molecular_functionproteasome binding
C0070842biological_processaggresome assembly
C1901990biological_processregulation of mitotic cell cycle phase transition
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Activation by thioester intermediate formation with UBA6
ChainResidueDetails
CGLY164
AASN505
AASP569
BARG46
BASN505
BASP569

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:35986001, ECO:0007744|PDB:7SOL
ChainResidueDetails
AALA470
AGLN509
BALA470
BGLN509

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:35970836, ECO:0000305|PubMed:35986001, ECO:0007744|PDB:7PVN, ECO:0007744|PDB:7SOL
ChainResidueDetails
AASP497
BASN570
AARG508
ALYS521
AVAL545
AASN570
BASP497
BARG508
BLYS521
BVAL545

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P22515
ChainResidueDetails
AASP499
AGLU502
BASP499
BGLU502

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330
ChainResidueDetails
AMET1
BMET1

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR54
BTHR54

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER301
BSER301

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS544
BLYS544
ALYS664
BLYS664

site_idSWS_FT_FI9
Number of Residues2
DetailsACT_SITE: Glycyl thioester intermediate => ECO:0000255|PROSITE-ProRule:PRU10132
ChainResidueDetails
AALA625
BALA625

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ATHR793
BTHR793

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231
ChainResidueDetails
ASER810
BSER810

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q02053
ChainResidueDetails
ASER816
BSER816

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER820
BSER820

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER835
BSER835

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PDB entries from 2025-06-11

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