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6JPQ

CryoEM structure of Abo1 hexamer - ADP complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000785cellular_componentchromatin
A0003682molecular_functionchromatin binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005694cellular_componentchromosome
A0006325biological_processchromatin organization
A0006334biological_processnucleosome assembly
A0006337biological_processnucleosome disassembly
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0042393molecular_functionhistone binding
A0045815biological_processtranscription initiation-coupled chromatin remodeling
A0140665molecular_functionATP-dependent H3-H4 histone complex chaperone activity
B0000785cellular_componentchromatin
B0003682molecular_functionchromatin binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005694cellular_componentchromosome
B0006325biological_processchromatin organization
B0006334biological_processnucleosome assembly
B0006337biological_processnucleosome disassembly
B0016787molecular_functionhydrolase activity
B0016887molecular_functionATP hydrolysis activity
B0042393molecular_functionhistone binding
B0045815biological_processtranscription initiation-coupled chromatin remodeling
B0140665molecular_functionATP-dependent H3-H4 histone complex chaperone activity
C0000785cellular_componentchromatin
C0003682molecular_functionchromatin binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005694cellular_componentchromosome
C0006325biological_processchromatin organization
C0006334biological_processnucleosome assembly
C0006337biological_processnucleosome disassembly
C0016787molecular_functionhydrolase activity
C0016887molecular_functionATP hydrolysis activity
C0042393molecular_functionhistone binding
C0045815biological_processtranscription initiation-coupled chromatin remodeling
C0140665molecular_functionATP-dependent H3-H4 histone complex chaperone activity
D0000785cellular_componentchromatin
D0003682molecular_functionchromatin binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0005694cellular_componentchromosome
D0006325biological_processchromatin organization
D0006334biological_processnucleosome assembly
D0006337biological_processnucleosome disassembly
D0016787molecular_functionhydrolase activity
D0016887molecular_functionATP hydrolysis activity
D0042393molecular_functionhistone binding
D0045815biological_processtranscription initiation-coupled chromatin remodeling
D0140665molecular_functionATP-dependent H3-H4 histone complex chaperone activity
E0000785cellular_componentchromatin
E0003682molecular_functionchromatin binding
E0005524molecular_functionATP binding
E0005634cellular_componentnucleus
E0005694cellular_componentchromosome
E0006325biological_processchromatin organization
E0006334biological_processnucleosome assembly
E0006337biological_processnucleosome disassembly
E0016787molecular_functionhydrolase activity
E0016887molecular_functionATP hydrolysis activity
E0042393molecular_functionhistone binding
E0045815biological_processtranscription initiation-coupled chromatin remodeling
E0140665molecular_functionATP-dependent H3-H4 histone complex chaperone activity
F0000785cellular_componentchromatin
F0003682molecular_functionchromatin binding
F0005524molecular_functionATP binding
F0005634cellular_componentnucleus
F0005694cellular_componentchromosome
F0006325biological_processchromatin organization
F0006334biological_processnucleosome assembly
F0006337biological_processnucleosome disassembly
F0016787molecular_functionhydrolase activity
F0016887molecular_functionATP hydrolysis activity
F0042393molecular_functionhistone binding
F0045815biological_processtranscription initiation-coupled chromatin remodeling
F0140665molecular_functionATP-dependent H3-H4 histone complex chaperone activity
Functional Information from PROSITE/UniProt
site_idPS00674
Number of Residues19
DetailsAAA AAA-protein family signature. ViIIgATNrpdaVDpALr.R
ChainResidueDetails
AVAL408-ARG426

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:31848341, ECO:0007744|PDB:6JQ0
ChainResidueDetails
APRO309
BPRO309
CPRO309
DPRO309
EPRO309
FPRO309

227344

PDB entries from 2024-11-13

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