8x19

Structure of nucleosome-bound SRCAP-C in the ADP-BeFx-bound state

Method: ELECTRON MICROSCOPY Dmax: 233.3 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Histone H2A type 1-C

Homo sapiens

UniProt Q93077

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 23 DNA 2 PDB declaration: 25-meric(25) Consistent with all polymer counts Chain A; UniProt 1–130 Chain E; UniProt 1–130 Not recorded Histone H2B type 1-C/E/F/G/I × 2 (P62807) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Helicase SRCAP × 1 (Q6ZRS2) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Actin-related protein 6 × 1 (Q9GZN1) Zinc finger HIT domain-containing protein 1 × 1 (O43257) RuvB-like 1 × 3 (Q9Y265) RuvB-like 2 × 3 (Q9Y230) Actin, cytoplasmic 1 × 2 (P60709) Actin-like protein 6A × 1 (O96019) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) YEATS domain-containing protein 4 × 1 (O95619) DNA (147-MER) × 1 DNA (147-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

25 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1C_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–130; UniProt 1–130 Author chain E; PDBConstruct 1–130; UniProt 1–130

Histone H2B type 1-C/E/F/G/I

Homo sapiens

UniProt P62807

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 23 DNA 2 PDB declaration: 25-meric(25) Consistent with all polymer counts Chain B; UniProt 1–126 Chain F; UniProt 1–126 Not recorded Histone H2A type 1-C × 2 (Q93077) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Helicase SRCAP × 1 (Q6ZRS2) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Actin-related protein 6 × 1 (Q9GZN1) Zinc finger HIT domain-containing protein 1 × 1 (O43257) RuvB-like 1 × 3 (Q9Y265) RuvB-like 2 × 3 (Q9Y230) Actin, cytoplasmic 1 × 2 (P60709) Actin-like protein 6A × 1 (O96019) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) YEATS domain-containing protein 4 × 1 (O95619) DNA (147-MER) × 1 DNA (147-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

79 other PDB entries and 79 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1C_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–126; UniProt 1–126 Author chain F; PDBConstruct 1–126; UniProt 1–126

Histone H3.1

Homo sapiens

UniProt P68431

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 23 DNA 2 PDB declaration: 25-meric(25) Consistent with all polymer counts Chain C; UniProt 1–136 Chain G; UniProt 1–136 Not recorded Histone H2A type 1-C × 2 (Q93077) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Histone H4 × 2 (P62805) Helicase SRCAP × 1 (Q6ZRS2) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Actin-related protein 6 × 1 (Q9GZN1) Zinc finger HIT domain-containing protein 1 × 1 (O43257) RuvB-like 1 × 3 (Q9Y265) RuvB-like 2 × 3 (Q9Y230) Actin, cytoplasmic 1 × 2 (P60709) Actin-like protein 6A × 1 (O96019) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) YEATS domain-containing protein 4 × 1 (O95619) DNA (147-MER) × 1 DNA (147-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

402 other PDB entries and 475 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H31_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–136; UniProt 1–136 Author chain G; PDBConstruct 1–136; UniProt 1–136

Histone H4

Homo sapiens

UniProt P62805

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 23 DNA 2 PDB declaration: 25-meric(25) Consistent with all polymer counts Chain D; UniProt 1–103 Chain H; UniProt 1–103 Not recorded Histone H2A type 1-C × 2 (Q93077) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Histone H3.1 × 2 (P68431) Helicase SRCAP × 1 (Q6ZRS2) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Actin-related protein 6 × 1 (Q9GZN1) Zinc finger HIT domain-containing protein 1 × 1 (O43257) RuvB-like 1 × 3 (Q9Y265) RuvB-like 2 × 3 (Q9Y230) Actin, cytoplasmic 1 × 2 (P60709) Actin-like protein 6A × 1 (O96019) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) YEATS domain-containing protein 4 × 1 (O95619) DNA (147-MER) × 1 DNA (147-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

581 other PDB entries and 633 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–103; UniProt 1–103 Author chain H; PDBConstruct 1–103; UniProt 1–103

Helicase SRCAP

Homo sapiens

UniProt Q6ZRS2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 23 DNA 2 PDB declaration: 25-meric(25) Consistent with all polymer counts Chain I; UniProt 1–3230 Not recorded Histone H2A type 1-C × 2 (Q93077) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Actin-related protein 6 × 1 (Q9GZN1) Zinc finger HIT domain-containing protein 1 × 1 (O43257) RuvB-like 1 × 3 (Q9Y265) RuvB-like 2 × 3 (Q9Y230) Actin, cytoplasmic 1 × 2 (P60709) Actin-like protein 6A × 1 (O96019) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) YEATS domain-containing protein 4 × 1 (O95619) DNA (147-MER) × 1 DNA (147-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SRCAP_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain I; PDBConstruct 1–3230; UniProt 1–3230

Vacuolar protein sorting-associated protein 72 homolog

Homo sapiens

UniProt Q15906

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 23 DNA 2 PDB declaration: 25-meric(25) Consistent with all polymer counts Chain J; UniProt 1–364 Not recorded Histone H2A type 1-C × 2 (Q93077) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Helicase SRCAP × 1 (Q6ZRS2) Actin-related protein 6 × 1 (Q9GZN1) Zinc finger HIT domain-containing protein 1 × 1 (O43257) RuvB-like 1 × 3 (Q9Y265) RuvB-like 2 × 3 (Q9Y230) Actin, cytoplasmic 1 × 2 (P60709) Actin-like protein 6A × 1 (O96019) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) YEATS domain-containing protein 4 × 1 (O95619) DNA (147-MER) × 1 DNA (147-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

16 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VPS72_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain J; PDBConstruct 1–364; UniProt 1–364

Actin-related protein 6

Homo sapiens

UniProt Q9GZN1

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 23 DNA 2 PDB declaration: 25-meric(25) Consistent with all polymer counts Chain K; UniProt 1–396 Not recorded Histone H2A type 1-C × 2 (Q93077) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Helicase SRCAP × 1 (Q6ZRS2) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Zinc finger HIT domain-containing protein 1 × 1 (O43257) RuvB-like 1 × 3 (Q9Y265) RuvB-like 2 × 3 (Q9Y230) Actin, cytoplasmic 1 × 2 (P60709) Actin-like protein 6A × 1 (O96019) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) YEATS domain-containing protein 4 × 1 (O95619) DNA (147-MER) × 1 DNA (147-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARP6_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain K; PDBConstruct 1–396; UniProt 1–396

Zinc finger HIT domain-containing protein 1

Homo sapiens

UniProt O43257

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 23 DNA 2 PDB declaration: 25-meric(25) Consistent with all polymer counts Chain L; UniProt 1–154 Not recorded Histone H2A type 1-C × 2 (Q93077) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Helicase SRCAP × 1 (Q6ZRS2) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Actin-related protein 6 × 1 (Q9GZN1) RuvB-like 1 × 3 (Q9Y265) RuvB-like 2 × 3 (Q9Y230) Actin, cytoplasmic 1 × 2 (P60709) Actin-like protein 6A × 1 (O96019) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) YEATS domain-containing protein 4 × 1 (O95619) DNA (147-MER) × 1 DNA (147-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ZNHI1_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain L; PDBConstruct 1–154; UniProt 1–154

RuvB-like 1

Homo sapiens

UniProt Q9Y265

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 23 DNA 2 PDB declaration: 25-meric(25) Consistent with all polymer counts Chain M; UniProt 1–456 Chain O; UniProt 1–456 Chain Q; UniProt 1–456 Not recorded Histone H2A type 1-C × 2 (Q93077) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Helicase SRCAP × 1 (Q6ZRS2) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Actin-related protein 6 × 1 (Q9GZN1) Zinc finger HIT domain-containing protein 1 × 1 (O43257) RuvB-like 2 × 3 (Q9Y230) Actin, cytoplasmic 1 × 2 (P60709) Actin-like protein 6A × 1 (O96019) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) YEATS domain-containing protein 4 × 1 (O95619) DNA (147-MER) × 1 DNA (147-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

35 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RUVB1_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain M; PDBConstruct 1–456; UniProt 1–456 Author chain O; PDBConstruct 1–456; UniProt 1–456 Author chain Q; PDBConstruct 1–456; UniProt 1–456

RuvB-like 2

Homo sapiens

UniProt Q9Y230

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 23 DNA 2 PDB declaration: 25-meric(25) Consistent with all polymer counts Chain N; UniProt 1–463 Chain P; UniProt 1–463 Chain R; UniProt 1–463 Not recorded Histone H2A type 1-C × 2 (Q93077) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Helicase SRCAP × 1 (Q6ZRS2) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Actin-related protein 6 × 1 (Q9GZN1) Zinc finger HIT domain-containing protein 1 × 1 (O43257) RuvB-like 1 × 3 (Q9Y265) Actin, cytoplasmic 1 × 2 (P60709) Actin-like protein 6A × 1 (O96019) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) YEATS domain-containing protein 4 × 1 (O95619) DNA (147-MER) × 1 DNA (147-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

37 other PDB entries and 39 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RUVB2_HUMAN
Isoform
PDB entities 10
Chains and sequence ranges Author chain N; PDBConstruct 1–463; UniProt 1–463 Author chain P; PDBConstruct 1–463; UniProt 1–463 Author chain R; PDBConstruct 1–463; UniProt 1–463

Actin, cytoplasmic 1

Homo sapiens

UniProt P60709

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 23 DNA 2 PDB declaration: 25-meric(25) Consistent with all polymer counts Chain S; UniProt 1–375 Chain U; UniProt 1–375 Not recorded Histone H2A type 1-C × 2 (Q93077) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Helicase SRCAP × 1 (Q6ZRS2) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Actin-related protein 6 × 1 (Q9GZN1) Zinc finger HIT domain-containing protein 1 × 1 (O43257) RuvB-like 1 × 3 (Q9Y265) RuvB-like 2 × 3 (Q9Y230) Actin-like protein 6A × 1 (O96019) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) YEATS domain-containing protein 4 × 1 (O95619) DNA (147-MER) × 1 DNA (147-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

72 other PDB entries and 83 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTB_HUMAN
Isoform
PDB entities 11
Chains and sequence ranges Author chain S; PDBConstruct 1–375; UniProt 1–375 Author chain U; PDBConstruct 1–375; UniProt 1–375

Actin-like protein 6A

Homo sapiens

UniProt O96019

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 23 DNA 2 PDB declaration: 25-meric(25) Consistent with all polymer counts Chain T; UniProt 1–429 Not recorded Histone H2A type 1-C × 2 (Q93077) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Helicase SRCAP × 1 (Q6ZRS2) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Actin-related protein 6 × 1 (Q9GZN1) Zinc finger HIT domain-containing protein 1 × 1 (O43257) RuvB-like 1 × 3 (Q9Y265) RuvB-like 2 × 3 (Q9Y230) Actin, cytoplasmic 1 × 2 (P60709) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) YEATS domain-containing protein 4 × 1 (O95619) DNA (147-MER) × 1 DNA (147-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

24 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACL6A_HUMAN
Isoform
PDB entities 12
Chains and sequence ranges Author chain T; PDBConstruct 1–429; UniProt 1–429

DNA methyltransferase 1-associated protein 1

Homo sapiens

UniProt Q9NPF5

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 23 DNA 2 PDB declaration: 25-meric(25) Consistent with all polymer counts Chain V; UniProt 1–467 Not recorded Histone H2A type 1-C × 2 (Q93077) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Helicase SRCAP × 1 (Q6ZRS2) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Actin-related protein 6 × 1 (Q9GZN1) Zinc finger HIT domain-containing protein 1 × 1 (O43257) RuvB-like 1 × 3 (Q9Y265) RuvB-like 2 × 3 (Q9Y230) Actin, cytoplasmic 1 × 2 (P60709) Actin-like protein 6A × 1 (O96019) YEATS domain-containing protein 4 × 1 (O95619) DNA (147-MER) × 1 DNA (147-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DMAP1_HUMAN
Isoform
PDB entities 13
Chains and sequence ranges Author chain V; PDBConstruct 1–467; UniProt 1–467

YEATS domain-containing protein 4

Homo sapiens

UniProt O95619

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 23 DNA 2 PDB declaration: 25-meric(25) Consistent with all polymer counts Chain W; UniProt 1–227 Not recorded Histone H2A type 1-C × 2 (Q93077) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Helicase SRCAP × 1 (Q6ZRS2) Vacuolar protein sorting-associated protein 72 homolog × 1 (Q15906) Actin-related protein 6 × 1 (Q9GZN1) Zinc finger HIT domain-containing protein 1 × 1 (O43257) RuvB-like 1 × 3 (Q9Y265) RuvB-like 2 × 3 (Q9Y230) Actin, cytoplasmic 1 × 2 (P60709) Actin-like protein 6A × 1 (O96019) DNA methyltransferase 1-associated protein 1 × 1 (Q9NPF5) DNA (147-MER) × 1 DNA (147-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

18 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name YETS4_HUMAN
Isoform
PDB entities 14
Chains and sequence ranges Author chain W; PDBConstruct 1–227; UniProt 1–227

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8x19

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8x19
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8x19
Deposition date deposition_date2023-11-06
Structure title titleStructure of nucleosome-bound SRCAP-C in the ADP-BeFx-bound state
Keywords keywordsRemodeler; SRCAP; H2A.Z, DNA BINDING PROTEIN/DNA, DNA BINDING PROTEIN-DNA complex; DNA BINDING PROTEIN/DNA
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier68.97
Radius of gyration Rg (electron density) rg_electron69.14
Forward intensity I(0) i010687200000.00
Molecular weight molecular_weight812910.0 kDa
Excluded volume excluded_volume991800 ų
Envelope volume envelope_volume1569200 ų
Hydration-shell volume shell_volume182710 ų
Envelope diameter envelope_diameter219.1
Shell Rg shell_rg76.12
Envelope Rg envelope_rg66.30
Shape Rg shape_rg69.17
Total Rg total_rg69.15
Total atoms total_atoms56704
Residues n_residues6666
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax233.3
Rg (real space) rg_real68.77
Rg uncertainty (real space) rg_real_error2.04
I(0) (real space) i0_real1.0690e+10
I(0) uncertainty (real space) i0_real_error2.4980e+08
Rg (reciprocal space) rg_reciprocal69.58
I(0) (reciprocal space) i0_reciprocal10700000000.0000
Solution quality estimate total_estimate0.8754
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary91.3
Skewness Skewness skewness0.125
Kurtosis Kurtosis kurtosis-0.541
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0007
Highest regularization parameter α highest_alpha660500000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.848; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.850

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (20)

8. Citations (1)

9. Files and Curves (10)