Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6JQ0

CryoEM structure of Abo1 Walker B (E372Q) mutant hexamer - ATP complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000785	cellular_component	chromatin
A	0003682	molecular_function	chromatin binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005694	cellular_component	chromosome
A	0006334	biological_process	nucleosome assembly
A	0006337	biological_process	nucleosome disassembly
A	0006338	biological_process	chromatin remodeling
A	0016787	molecular_function	hydrolase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0042393	molecular_function	histone binding
A	0045815	biological_process	transcription initiation-coupled chromatin remodeling
A	0140665	molecular_function	ATP-dependent H3-H4 histone complex chaperone activity
B	0000785	cellular_component	chromatin
B	0003682	molecular_function	chromatin binding
B	0005524	molecular_function	ATP binding
B	0005634	cellular_component	nucleus
B	0005694	cellular_component	chromosome
B	0006334	biological_process	nucleosome assembly
B	0006337	biological_process	nucleosome disassembly
B	0006338	biological_process	chromatin remodeling
B	0016787	molecular_function	hydrolase activity
B	0016887	molecular_function	ATP hydrolysis activity
B	0042393	molecular_function	histone binding
B	0045815	biological_process	transcription initiation-coupled chromatin remodeling
B	0140665	molecular_function	ATP-dependent H3-H4 histone complex chaperone activity
C	0000785	cellular_component	chromatin
C	0003682	molecular_function	chromatin binding
C	0005524	molecular_function	ATP binding
C	0005634	cellular_component	nucleus
C	0005694	cellular_component	chromosome
C	0006334	biological_process	nucleosome assembly
C	0006337	biological_process	nucleosome disassembly
C	0006338	biological_process	chromatin remodeling
C	0016787	molecular_function	hydrolase activity
C	0016887	molecular_function	ATP hydrolysis activity
C	0042393	molecular_function	histone binding
C	0045815	biological_process	transcription initiation-coupled chromatin remodeling
C	0140665	molecular_function	ATP-dependent H3-H4 histone complex chaperone activity
D	0000785	cellular_component	chromatin
D	0003682	molecular_function	chromatin binding
D	0005524	molecular_function	ATP binding
D	0005634	cellular_component	nucleus
D	0005694	cellular_component	chromosome
D	0006334	biological_process	nucleosome assembly
D	0006337	biological_process	nucleosome disassembly
D	0006338	biological_process	chromatin remodeling
D	0016787	molecular_function	hydrolase activity
D	0016887	molecular_function	ATP hydrolysis activity
D	0042393	molecular_function	histone binding
D	0045815	biological_process	transcription initiation-coupled chromatin remodeling
D	0140665	molecular_function	ATP-dependent H3-H4 histone complex chaperone activity
E	0000785	cellular_component	chromatin
E	0003682	molecular_function	chromatin binding
E	0005524	molecular_function	ATP binding
E	0005634	cellular_component	nucleus
E	0005694	cellular_component	chromosome
E	0006334	biological_process	nucleosome assembly
E	0006337	biological_process	nucleosome disassembly
E	0006338	biological_process	chromatin remodeling
E	0016787	molecular_function	hydrolase activity
E	0016887	molecular_function	ATP hydrolysis activity
E	0042393	molecular_function	histone binding
E	0045815	biological_process	transcription initiation-coupled chromatin remodeling
E	0140665	molecular_function	ATP-dependent H3-H4 histone complex chaperone activity
F	0000785	cellular_component	chromatin
F	0003682	molecular_function	chromatin binding
F	0005524	molecular_function	ATP binding
F	0005634	cellular_component	nucleus
F	0005694	cellular_component	chromosome
F	0006334	biological_process	nucleosome assembly
F	0006337	biological_process	nucleosome disassembly
F	0006338	biological_process	chromatin remodeling
F	0016787	molecular_function	hydrolase activity
F	0016887	molecular_function	ATP hydrolysis activity
F	0042393	molecular_function	histone binding
F	0045815	biological_process	transcription initiation-coupled chromatin remodeling
F	0140665	molecular_function	ATP-dependent H3-H4 histone complex chaperone activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue ADP A 1201

Chain	Residue
A	SER267
A	ILE447
A	GLY476
A	GLY269
A	PRO309
A	GLY310
A	THR311
A	GLY312
A	LYS313
A	THR314
A	LEU315

site_id	AC2
Number of Residues	13
Details	binding site for residue ATP B 1201

Chain	Residue
A	ARG426
A	ARG429
B	GLY269
B	PRO309
B	GLY310
B	THR311
B	GLY312
B	LYS313
B	THR314
B	LEU315
B	ILE447
B	HIS451
B	GLY476

site_id	AC3
Number of Residues	14
Details	binding site for Di-peptide ATP C 1201 and GLY C 310

Chain	Residue
B	ARG426
B	ARG429
C	GLY269
C	PRO308
C	PRO309
C	THR311
C	GLY312
C	LYS313
C	THR314
C	ASN415
C	ILE447
C	HIS451
C	GLY476
C	ALA477

site_id	AC4
Number of Residues	19
Details	binding site for Di-peptide ATP C 1201 and LYS C 313

Chain	Residue
B	ARG426
B	ARG429
C	GLY269
C	GLY307
C	PRO308
C	PRO309
C	GLY310
C	THR311
C	GLY312
C	THR314
C	LEU315
C	MET316
C	THR414
C	ASN415
C	PHE436
C	ILE447
C	HIS451
C	GLY476
C	ALA477

site_id	AC5
Number of Residues	20
Details	binding site for Di-peptide ATP C 1201 and ILE C 447

Chain	Residue
B	ARG426
B	ARG429
C	GLY269
C	PRO309
C	GLY310
C	THR311
C	GLY312
C	LYS313
C	THR314
C	ASN415
C	ALA443
C	ARG444
C	LYS445
C	LYS446
C	ILE448
C	GLU449
C	HIS451
C	GLY476
C	ALA477
C	LEU479

site_id	AC6
Number of Residues	14
Details	binding site for Di-peptide ATP C 1201 and GLY C 476

Chain	Residue
B	ARG426
B	ARG429
C	GLY269
C	PRO309
C	GLY310
C	THR311
C	GLY312
C	LYS313
C	THR314
C	ASN415
C	ILE447
C	HIS451
C	GLY475
C	ALA477

site_id	AC7
Number of Residues	15
Details	binding site for Di-peptide ATP D 1201 and LYS D 313

Chain	Residue
D	THR314
D	LEU315
D	MET316
D	ASN415
D	ILE447
D	HIS451
D	GLY476
C	ARG426
C	ARG429
D	GLY307
D	PRO308
D	PRO309
D	GLY310
D	THR311
D	GLY312

site_id	AC8
Number of Residues	17
Details	binding site for Di-peptide ATP D 1201 and ILE D 447

Chain	Residue
C	ARG426
C	ARG429
D	PRO309
D	GLY310
D	THR311
D	GLY312
D	LYS313
D	THR314
D	ASN415
D	ALA443
D	LYS445
D	LYS446
D	ILE448
D	GLU449
D	ILE450
D	HIS451
D	GLY476

site_id	AC9
Number of Residues	15
Details	binding site for Di-peptide ATP D 1201 and HIS D 451

Chain	Residue
C	ARG426
C	ARG429
D	PRO309
D	GLY310
D	THR311
D	GLY312
D	LYS313
D	THR314
D	ASN415
D	ILE447
D	GLU449
D	ILE450
D	THR452
D	GLY476
D	ARG480

site_id	AD1
Number of Residues	13
Details	binding site for Di-peptide ATP D 1201 and GLY D 310

Chain	Residue
C	ARG426
C	ARG429
D	PRO308
D	PRO309
D	THR311
D	GLY312
D	LYS313
D	THR314
D	ASN415
D	ILE447
D	HIS451
D	GLY476
D	ALA477

site_id	AD2
Number of Residues	20
Details	binding site for Di-peptide ATP E 1201 and LYS E 313

Chain	Residue
D	ARG426
D	ARG429
E	GLY269
E	PHE305
E	HIS306
E	GLY307
E	PRO308
E	PRO309
E	GLY310
E	THR311
E	GLY312
E	THR314
E	MET316
E	ALA317
E	THR414
E	ASN415
E	PHE436
E	ILE447
E	HIS451
E	GLY476

site_id	AD3
Number of Residues	20
Details	binding site for Di-peptide ATP E 1201 and ILE E 447

Chain	Residue
D	ARG426
D	ARG429
E	GLY269
E	PRO308
E	PRO309
E	GLY310
E	THR311
E	GLY312
E	LYS313
E	THR314
E	ASN415
E	ALA443
E	ARG444
E	LYS445
E	LYS446
E	ILE448
E	GLU449
E	HIS451
E	GLY476
E	LEU479

site_id	AD4
Number of Residues	18
Details	binding site for Di-peptide ATP E 1201 and HIS E 451

Chain	Residue
D	ARG426
D	ARG429
E	GLY269
E	PRO308
E	PRO309
E	GLY310
E	THR311
E	GLY312
E	LYS313
E	THR314
E	ASN415
E	ILE447
E	GLU449
E	ILE450
E	THR452
E	ARG453
E	GLY476
E	ARG480

site_id	AD5
Number of Residues	14
Details	binding site for Di-peptide ATP E 1201 and GLY E 310

Chain	Residue
D	ARG426
D	ARG429
E	GLY269
E	PRO308
E	PRO309
E	THR311
E	GLY312
E	LYS313
E	THR314
E	ASN415
E	ILE447
E	HIS451
E	GLY476
E	ALA477

site_id	AD6
Number of Residues	20
Details	binding site for Di-peptide ATP F 1201 and LYS F 313

Chain	Residue
E	ARG426
E	ARG429
F	GLY269
F	HIS306
F	GLY307
F	PRO308
F	PRO309
F	GLY310
F	THR311
F	GLY312
F	THR314
F	LEU315
F	MET316
F	ALA317
F	THR414
F	ASN415
F	PHE436
F	ILE447
F	HIS451
F	GLY476

site_id	AD7
Number of Residues	18
Details	binding site for Di-peptide ATP F 1201 and ILE F 447

Chain	Residue
E	ARG426
E	ARG429
F	GLY269
F	PRO308
F	PRO309
F	GLY310
F	THR311
F	GLY312
F	LYS313
F	THR314
F	ALA443
F	LYS445
F	LYS446
F	ILE448
F	GLU449
F	ILE450
F	HIS451
F	GLY476

site_id	AD8
Number of Residues	16
Details	binding site for Di-peptide ATP F 1201 and HIS F 451

Chain	Residue
E	ARG426
E	ARG429
F	GLY269
F	PRO308
F	PRO309
F	GLY310
F	THR311
F	GLY312
F	LYS313
F	THR314
F	ILE447
F	GLU449
F	ILE450
F	THR452
F	GLY476
F	ARG480

site_id	AD9
Number of Residues	13
Details	binding site for Di-peptide ATP F 1201 and GLY F 310

Chain	Residue
E	ARG426
E	ARG429
F	GLY269
F	PRO308
F	PRO309
F	THR311
F	GLY312
F	LYS313
F	THR314
F	ILE447
F	HIS451
F	GLY476
F	ALA477

Functional Information from PROSITE/UniProt

site_id	PS00674
Number of Residues	19
Details	AAA AAA-protein family signature. ViIIgATNrpdaVDpALr.R

Chain	Residue	Details
A	VAL408-ARG426

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:31848341, ECO:0007744\|PDB:6JQ0

Chain	Residue	Details
A	PRO309
B	PRO309
C	PRO309
D	PRO309
E	PRO309
F	PRO309

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)