9ii7

RNA polymerase II elongation complex stalled at SHL(-1) of the nucleosome containing histone variant H2A.B

Method: ELECTRON MICROSCOPY Dmax: 200.2 Å Quality: REASONABLE

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

DNA-directed RNA polymerase subunit

OrganismNot specified

UniProt C4R4Y0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 21 DNA 2 RNA 1 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain A; UniProt 1–1743 Not recorded DNA-directed RNA polymerase subunit beta × 1 (C4QZQ7) RNA polymerase II third largest subunit B44, part of central core × 1 (C4R7L2) RNA polymerase II subunit B32 × 1 (C4R2U9) DNA-directed RNA polymerases I, II, and III subunit RPABC1 × 1 (C4R3P8) RNA polymerase subunit ABC23, common to RNA polymerases I, II, and III × 1 (C4R1V1) RNA polymerase II subunit × 1 (C4R9A1) DNA-directed RNA polymerases I, II, and III subunit RPABC3 × 1 (C4R273) DNA-directed RNA polymerase subunit × 1 (F2QPE6) RNA polymerase subunit ABC10-beta, common to RNA polymerases I, II, and III × 1 (C4R009) RNA polymerase II subunit B12.5 × 1 (C4R3Z5) RNA polymerase subunit ABC10-alpha × 1 (F2QMI1) Transcription elongation factor 1 homolog × 1 (C4QZ45) DNA (198-MER) × 1 ;RNA (5'-R(P*CP*CP*CP*GP*GP*UP*GP*UP*CP*UP*UP*GP*GP*GP*UP*G)-3') ; × 1 DNA (198-MER) × 1 Transcription elongation factor SPT4 × 1 (F2QTA2) Transcription elongation factor SPT5 × 1 (C4R370) Histone H3.3 × 2 (P84243) Histone H4 × 2 (P62805) Histone H2A-Bbd type 2/3 × 1 (P0C5Z0) Histone H2B type 1-J × 1 (P06899) ZN ZINC ION × 10 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES-KOH(pH7.5), 200 nM Zinc acetate, 0.1 mM TCEP-HCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

44 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C4R4Y0_KOMPG
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1743; UniProt 1–1743

DNA-directed RNA polymerase subunit beta

OrganismNot specified

UniProt C4QZQ7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 21 DNA 2 RNA 1 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain B; UniProt 1–1227 Not recorded DNA-directed RNA polymerase subunit × 1 (C4R4Y0) RNA polymerase II third largest subunit B44, part of central core × 1 (C4R7L2) RNA polymerase II subunit B32 × 1 (C4R2U9) DNA-directed RNA polymerases I, II, and III subunit RPABC1 × 1 (C4R3P8) RNA polymerase subunit ABC23, common to RNA polymerases I, II, and III × 1 (C4R1V1) RNA polymerase II subunit × 1 (C4R9A1) DNA-directed RNA polymerases I, II, and III subunit RPABC3 × 1 (C4R273) DNA-directed RNA polymerase subunit × 1 (F2QPE6) RNA polymerase subunit ABC10-beta, common to RNA polymerases I, II, and III × 1 (C4R009) RNA polymerase II subunit B12.5 × 1 (C4R3Z5) RNA polymerase subunit ABC10-alpha × 1 (F2QMI1) Transcription elongation factor 1 homolog × 1 (C4QZ45) DNA (198-MER) × 1 ;RNA (5'-R(P*CP*CP*CP*GP*GP*UP*GP*UP*CP*UP*UP*GP*GP*GP*UP*G)-3') ; × 1 DNA (198-MER) × 1 Transcription elongation factor SPT4 × 1 (F2QTA2) Transcription elongation factor SPT5 × 1 (C4R370) Histone H3.3 × 2 (P84243) Histone H4 × 2 (P62805) Histone H2A-Bbd type 2/3 × 1 (P0C5Z0) Histone H2B type 1-J × 1 (P06899) ZN ZINC ION × 10 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES-KOH(pH7.5), 200 nM Zinc acetate, 0.1 mM TCEP-HCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

44 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C4QZQ7_KOMPG
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–1227; UniProt 1–1227

RNA polymerase II third largest subunit B44, part of central core

OrganismNot specified

UniProt C4R7L2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 21 DNA 2 RNA 1 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain C; UniProt 1–304 Not recorded DNA-directed RNA polymerase subunit × 1 (C4R4Y0) DNA-directed RNA polymerase subunit beta × 1 (C4QZQ7) RNA polymerase II subunit B32 × 1 (C4R2U9) DNA-directed RNA polymerases I, II, and III subunit RPABC1 × 1 (C4R3P8) RNA polymerase subunit ABC23, common to RNA polymerases I, II, and III × 1 (C4R1V1) RNA polymerase II subunit × 1 (C4R9A1) DNA-directed RNA polymerases I, II, and III subunit RPABC3 × 1 (C4R273) DNA-directed RNA polymerase subunit × 1 (F2QPE6) RNA polymerase subunit ABC10-beta, common to RNA polymerases I, II, and III × 1 (C4R009) RNA polymerase II subunit B12.5 × 1 (C4R3Z5) RNA polymerase subunit ABC10-alpha × 1 (F2QMI1) Transcription elongation factor 1 homolog × 1 (C4QZ45) DNA (198-MER) × 1 ;RNA (5'-R(P*CP*CP*CP*GP*GP*UP*GP*UP*CP*UP*UP*GP*GP*GP*UP*G)-3') ; × 1 DNA (198-MER) × 1 Transcription elongation factor SPT4 × 1 (F2QTA2) Transcription elongation factor SPT5 × 1 (C4R370) Histone H3.3 × 2 (P84243) Histone H4 × 2 (P62805) Histone H2A-Bbd type 2/3 × 1 (P0C5Z0) Histone H2B type 1-J × 1 (P06899) ZN ZINC ION × 10 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES-KOH(pH7.5), 200 nM Zinc acetate, 0.1 mM TCEP-HCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

44 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C4R7L2_KOMPG
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–304; UniProt 1–304

RNA polymerase II subunit B32

OrganismNot specified

UniProt C4R2U9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 21 DNA 2 RNA 1 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain D; UniProt 1–186 Not recorded DNA-directed RNA polymerase subunit × 1 (C4R4Y0) DNA-directed RNA polymerase subunit beta × 1 (C4QZQ7) RNA polymerase II third largest subunit B44, part of central core × 1 (C4R7L2) DNA-directed RNA polymerases I, II, and III subunit RPABC1 × 1 (C4R3P8) RNA polymerase subunit ABC23, common to RNA polymerases I, II, and III × 1 (C4R1V1) RNA polymerase II subunit × 1 (C4R9A1) DNA-directed RNA polymerases I, II, and III subunit RPABC3 × 1 (C4R273) DNA-directed RNA polymerase subunit × 1 (F2QPE6) RNA polymerase subunit ABC10-beta, common to RNA polymerases I, II, and III × 1 (C4R009) RNA polymerase II subunit B12.5 × 1 (C4R3Z5) RNA polymerase subunit ABC10-alpha × 1 (F2QMI1) Transcription elongation factor 1 homolog × 1 (C4QZ45) DNA (198-MER) × 1 ;RNA (5'-R(P*CP*CP*CP*GP*GP*UP*GP*UP*CP*UP*UP*GP*GP*GP*UP*G)-3') ; × 1 DNA (198-MER) × 1 Transcription elongation factor SPT4 × 1 (F2QTA2) Transcription elongation factor SPT5 × 1 (C4R370) Histone H3.3 × 2 (P84243) Histone H4 × 2 (P62805) Histone H2A-Bbd type 2/3 × 1 (P0C5Z0) Histone H2B type 1-J × 1 (P06899) ZN ZINC ION × 10 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES-KOH(pH7.5), 200 nM Zinc acetate, 0.1 mM TCEP-HCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

44 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C4R2U9_KOMPG
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–186; UniProt 1–186

DNA-directed RNA polymerases I, II, and III subunit RPABC1

OrganismNot specified

UniProt C4R3P8

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 21 DNA 2 RNA 1 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain E; UniProt 1–214 Not recorded DNA-directed RNA polymerase subunit × 1 (C4R4Y0) DNA-directed RNA polymerase subunit beta × 1 (C4QZQ7) RNA polymerase II third largest subunit B44, part of central core × 1 (C4R7L2) RNA polymerase II subunit B32 × 1 (C4R2U9) RNA polymerase subunit ABC23, common to RNA polymerases I, II, and III × 1 (C4R1V1) RNA polymerase II subunit × 1 (C4R9A1) DNA-directed RNA polymerases I, II, and III subunit RPABC3 × 1 (C4R273) DNA-directed RNA polymerase subunit × 1 (F2QPE6) RNA polymerase subunit ABC10-beta, common to RNA polymerases I, II, and III × 1 (C4R009) RNA polymerase II subunit B12.5 × 1 (C4R3Z5) RNA polymerase subunit ABC10-alpha × 1 (F2QMI1) Transcription elongation factor 1 homolog × 1 (C4QZ45) DNA (198-MER) × 1 ;RNA (5'-R(P*CP*CP*CP*GP*GP*UP*GP*UP*CP*UP*UP*GP*GP*GP*UP*G)-3') ; × 1 DNA (198-MER) × 1 Transcription elongation factor SPT4 × 1 (F2QTA2) Transcription elongation factor SPT5 × 1 (C4R370) Histone H3.3 × 2 (P84243) Histone H4 × 2 (P62805) Histone H2A-Bbd type 2/3 × 1 (P0C5Z0) Histone H2B type 1-J × 1 (P06899) ZN ZINC ION × 10 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES-KOH(pH7.5), 200 nM Zinc acetate, 0.1 mM TCEP-HCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

43 other PDB entries and 45 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C4R3P8_KOMPG
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–214; UniProt 1–214

RNA polymerase subunit ABC23, common to RNA polymerases I, II, and III

OrganismNot specified

UniProt C4R1V1

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 21 DNA 2 RNA 1 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain F; UniProt 1–155 Not recorded DNA-directed RNA polymerase subunit × 1 (C4R4Y0) DNA-directed RNA polymerase subunit beta × 1 (C4QZQ7) RNA polymerase II third largest subunit B44, part of central core × 1 (C4R7L2) RNA polymerase II subunit B32 × 1 (C4R2U9) DNA-directed RNA polymerases I, II, and III subunit RPABC1 × 1 (C4R3P8) RNA polymerase II subunit × 1 (C4R9A1) DNA-directed RNA polymerases I, II, and III subunit RPABC3 × 1 (C4R273) DNA-directed RNA polymerase subunit × 1 (F2QPE6) RNA polymerase subunit ABC10-beta, common to RNA polymerases I, II, and III × 1 (C4R009) RNA polymerase II subunit B12.5 × 1 (C4R3Z5) RNA polymerase subunit ABC10-alpha × 1 (F2QMI1) Transcription elongation factor 1 homolog × 1 (C4QZ45) DNA (198-MER) × 1 ;RNA (5'-R(P*CP*CP*CP*GP*GP*UP*GP*UP*CP*UP*UP*GP*GP*GP*UP*G)-3') ; × 1 DNA (198-MER) × 1 Transcription elongation factor SPT4 × 1 (F2QTA2) Transcription elongation factor SPT5 × 1 (C4R370) Histone H3.3 × 2 (P84243) Histone H4 × 2 (P62805) Histone H2A-Bbd type 2/3 × 1 (P0C5Z0) Histone H2B type 1-J × 1 (P06899) ZN ZINC ION × 10 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES-KOH(pH7.5), 200 nM Zinc acetate, 0.1 mM TCEP-HCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

44 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C4R1V1_KOMPG
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–155; UniProt 1–155

RNA polymerase II subunit

OrganismNot specified

UniProt C4R9A1

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 21 DNA 2 RNA 1 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain G; UniProt 1–171 Not recorded DNA-directed RNA polymerase subunit × 1 (C4R4Y0) DNA-directed RNA polymerase subunit beta × 1 (C4QZQ7) RNA polymerase II third largest subunit B44, part of central core × 1 (C4R7L2) RNA polymerase II subunit B32 × 1 (C4R2U9) DNA-directed RNA polymerases I, II, and III subunit RPABC1 × 1 (C4R3P8) RNA polymerase subunit ABC23, common to RNA polymerases I, II, and III × 1 (C4R1V1) DNA-directed RNA polymerases I, II, and III subunit RPABC3 × 1 (C4R273) DNA-directed RNA polymerase subunit × 1 (F2QPE6) RNA polymerase subunit ABC10-beta, common to RNA polymerases I, II, and III × 1 (C4R009) RNA polymerase II subunit B12.5 × 1 (C4R3Z5) RNA polymerase subunit ABC10-alpha × 1 (F2QMI1) Transcription elongation factor 1 homolog × 1 (C4QZ45) DNA (198-MER) × 1 ;RNA (5'-R(P*CP*CP*CP*GP*GP*UP*GP*UP*CP*UP*UP*GP*GP*GP*UP*G)-3') ; × 1 DNA (198-MER) × 1 Transcription elongation factor SPT4 × 1 (F2QTA2) Transcription elongation factor SPT5 × 1 (C4R370) Histone H3.3 × 2 (P84243) Histone H4 × 2 (P62805) Histone H2A-Bbd type 2/3 × 1 (P0C5Z0) Histone H2B type 1-J × 1 (P06899) ZN ZINC ION × 10 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES-KOH(pH7.5), 200 nM Zinc acetate, 0.1 mM TCEP-HCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

44 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C4R9A1_KOMPG
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–171; UniProt 1–171

DNA-directed RNA polymerases I, II, and III subunit RPABC3

OrganismNot specified

UniProt C4R273

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 21 DNA 2 RNA 1 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain H; UniProt 1–145 Not recorded DNA-directed RNA polymerase subunit × 1 (C4R4Y0) DNA-directed RNA polymerase subunit beta × 1 (C4QZQ7) RNA polymerase II third largest subunit B44, part of central core × 1 (C4R7L2) RNA polymerase II subunit B32 × 1 (C4R2U9) DNA-directed RNA polymerases I, II, and III subunit RPABC1 × 1 (C4R3P8) RNA polymerase subunit ABC23, common to RNA polymerases I, II, and III × 1 (C4R1V1) RNA polymerase II subunit × 1 (C4R9A1) DNA-directed RNA polymerase subunit × 1 (F2QPE6) RNA polymerase subunit ABC10-beta, common to RNA polymerases I, II, and III × 1 (C4R009) RNA polymerase II subunit B12.5 × 1 (C4R3Z5) RNA polymerase subunit ABC10-alpha × 1 (F2QMI1) Transcription elongation factor 1 homolog × 1 (C4QZ45) DNA (198-MER) × 1 ;RNA (5'-R(P*CP*CP*CP*GP*GP*UP*GP*UP*CP*UP*UP*GP*GP*GP*UP*G)-3') ; × 1 DNA (198-MER) × 1 Transcription elongation factor SPT4 × 1 (F2QTA2) Transcription elongation factor SPT5 × 1 (C4R370) Histone H3.3 × 2 (P84243) Histone H4 × 2 (P62805) Histone H2A-Bbd type 2/3 × 1 (P0C5Z0) Histone H2B type 1-J × 1 (P06899) ZN ZINC ION × 10 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES-KOH(pH7.5), 200 nM Zinc acetate, 0.1 mM TCEP-HCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

44 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C4R273_KOMPG
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–145; UniProt 1–145

DNA-directed RNA polymerase subunit

OrganismNot specified

UniProt F2QPE6

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 21 DNA 2 RNA 1 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain I; UniProt 1–115 Not recorded DNA-directed RNA polymerase subunit × 1 (C4R4Y0) DNA-directed RNA polymerase subunit beta × 1 (C4QZQ7) RNA polymerase II third largest subunit B44, part of central core × 1 (C4R7L2) RNA polymerase II subunit B32 × 1 (C4R2U9) DNA-directed RNA polymerases I, II, and III subunit RPABC1 × 1 (C4R3P8) RNA polymerase subunit ABC23, common to RNA polymerases I, II, and III × 1 (C4R1V1) RNA polymerase II subunit × 1 (C4R9A1) DNA-directed RNA polymerases I, II, and III subunit RPABC3 × 1 (C4R273) RNA polymerase subunit ABC10-beta, common to RNA polymerases I, II, and III × 1 (C4R009) RNA polymerase II subunit B12.5 × 1 (C4R3Z5) RNA polymerase subunit ABC10-alpha × 1 (F2QMI1) Transcription elongation factor 1 homolog × 1 (C4QZ45) DNA (198-MER) × 1 ;RNA (5'-R(P*CP*CP*CP*GP*GP*UP*GP*UP*CP*UP*UP*GP*GP*GP*UP*G)-3') ; × 1 DNA (198-MER) × 1 Transcription elongation factor SPT4 × 1 (F2QTA2) Transcription elongation factor SPT5 × 1 (C4R370) Histone H3.3 × 2 (P84243) Histone H4 × 2 (P62805) Histone H2A-Bbd type 2/3 × 1 (P0C5Z0) Histone H2B type 1-J × 1 (P06899) ZN ZINC ION × 10 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES-KOH(pH7.5), 200 nM Zinc acetate, 0.1 mM TCEP-HCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

43 other PDB entries and 45 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name F2QPE6_KOMPC
Isoform
PDB entities 9
Chains and sequence ranges Author chain I; PDBConstruct 1–115; UniProt 1–115

RNA polymerase subunit ABC10-beta, common to RNA polymerases I, II, and III

OrganismNot specified

UniProt C4R009

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 21 DNA 2 RNA 1 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain J; UniProt 1–72 Not recorded DNA-directed RNA polymerase subunit × 1 (C4R4Y0) DNA-directed RNA polymerase subunit beta × 1 (C4QZQ7) RNA polymerase II third largest subunit B44, part of central core × 1 (C4R7L2) RNA polymerase II subunit B32 × 1 (C4R2U9) DNA-directed RNA polymerases I, II, and III subunit RPABC1 × 1 (C4R3P8) RNA polymerase subunit ABC23, common to RNA polymerases I, II, and III × 1 (C4R1V1) RNA polymerase II subunit × 1 (C4R9A1) DNA-directed RNA polymerases I, II, and III subunit RPABC3 × 1 (C4R273) DNA-directed RNA polymerase subunit × 1 (F2QPE6) RNA polymerase II subunit B12.5 × 1 (C4R3Z5) RNA polymerase subunit ABC10-alpha × 1 (F2QMI1) Transcription elongation factor 1 homolog × 1 (C4QZ45) DNA (198-MER) × 1 ;RNA (5'-R(P*CP*CP*CP*GP*GP*UP*GP*UP*CP*UP*UP*GP*GP*GP*UP*G)-3') ; × 1 DNA (198-MER) × 1 Transcription elongation factor SPT4 × 1 (F2QTA2) Transcription elongation factor SPT5 × 1 (C4R370) Histone H3.3 × 2 (P84243) Histone H4 × 2 (P62805) Histone H2A-Bbd type 2/3 × 1 (P0C5Z0) Histone H2B type 1-J × 1 (P06899) ZN ZINC ION × 10 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES-KOH(pH7.5), 200 nM Zinc acetate, 0.1 mM TCEP-HCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

43 other PDB entries and 45 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C4R009_KOMPG
Isoform
PDB entities 10
Chains and sequence ranges Author chain J; PDBConstruct 1–72; UniProt 1–72

RNA polymerase II subunit B12.5

OrganismNot specified

UniProt C4R3Z5

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 21 DNA 2 RNA 1 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain K; UniProt 1–118 Not recorded DNA-directed RNA polymerase subunit × 1 (C4R4Y0) DNA-directed RNA polymerase subunit beta × 1 (C4QZQ7) RNA polymerase II third largest subunit B44, part of central core × 1 (C4R7L2) RNA polymerase II subunit B32 × 1 (C4R2U9) DNA-directed RNA polymerases I, II, and III subunit RPABC1 × 1 (C4R3P8) RNA polymerase subunit ABC23, common to RNA polymerases I, II, and III × 1 (C4R1V1) RNA polymerase II subunit × 1 (C4R9A1) DNA-directed RNA polymerases I, II, and III subunit RPABC3 × 1 (C4R273) DNA-directed RNA polymerase subunit × 1 (F2QPE6) RNA polymerase subunit ABC10-beta, common to RNA polymerases I, II, and III × 1 (C4R009) RNA polymerase subunit ABC10-alpha × 1 (F2QMI1) Transcription elongation factor 1 homolog × 1 (C4QZ45) DNA (198-MER) × 1 ;RNA (5'-R(P*CP*CP*CP*GP*GP*UP*GP*UP*CP*UP*UP*GP*GP*GP*UP*G)-3') ; × 1 DNA (198-MER) × 1 Transcription elongation factor SPT4 × 1 (F2QTA2) Transcription elongation factor SPT5 × 1 (C4R370) Histone H3.3 × 2 (P84243) Histone H4 × 2 (P62805) Histone H2A-Bbd type 2/3 × 1 (P0C5Z0) Histone H2B type 1-J × 1 (P06899) ZN ZINC ION × 10 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES-KOH(pH7.5), 200 nM Zinc acetate, 0.1 mM TCEP-HCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

44 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C4R3Z5_KOMPG
Isoform
PDB entities 11
Chains and sequence ranges Author chain K; PDBConstruct 1–118; UniProt 1–118

RNA polymerase subunit ABC10-alpha

OrganismNot specified

UniProt F2QMI1

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 21 DNA 2 RNA 1 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain L; UniProt 1–72 Not recorded DNA-directed RNA polymerase subunit × 1 (C4R4Y0) DNA-directed RNA polymerase subunit beta × 1 (C4QZQ7) RNA polymerase II third largest subunit B44, part of central core × 1 (C4R7L2) RNA polymerase II subunit B32 × 1 (C4R2U9) DNA-directed RNA polymerases I, II, and III subunit RPABC1 × 1 (C4R3P8) RNA polymerase subunit ABC23, common to RNA polymerases I, II, and III × 1 (C4R1V1) RNA polymerase II subunit × 1 (C4R9A1) DNA-directed RNA polymerases I, II, and III subunit RPABC3 × 1 (C4R273) DNA-directed RNA polymerase subunit × 1 (F2QPE6) RNA polymerase subunit ABC10-beta, common to RNA polymerases I, II, and III × 1 (C4R009) RNA polymerase II subunit B12.5 × 1 (C4R3Z5) Transcription elongation factor 1 homolog × 1 (C4QZ45) DNA (198-MER) × 1 ;RNA (5'-R(P*CP*CP*CP*GP*GP*UP*GP*UP*CP*UP*UP*GP*GP*GP*UP*G)-3') ; × 1 DNA (198-MER) × 1 Transcription elongation factor SPT4 × 1 (F2QTA2) Transcription elongation factor SPT5 × 1 (C4R370) Histone H3.3 × 2 (P84243) Histone H4 × 2 (P62805) Histone H2A-Bbd type 2/3 × 1 (P0C5Z0) Histone H2B type 1-J × 1 (P06899) ZN ZINC ION × 10 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES-KOH(pH7.5), 200 nM Zinc acetate, 0.1 mM TCEP-HCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

40 other PDB entries and 40 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name F2QMI1_KOMPC
Isoform
PDB entities 12
Chains and sequence ranges Author chain L; PDBConstruct 1–72; UniProt 1–72

Transcription elongation factor 1 homolog

Komagataella phaffii

UniProt C4QZ45

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 21 DNA 2 RNA 1 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain M; UniProt 1–110 Not recorded DNA-directed RNA polymerase subunit × 1 (C4R4Y0) DNA-directed RNA polymerase subunit beta × 1 (C4QZQ7) RNA polymerase II third largest subunit B44, part of central core × 1 (C4R7L2) RNA polymerase II subunit B32 × 1 (C4R2U9) DNA-directed RNA polymerases I, II, and III subunit RPABC1 × 1 (C4R3P8) RNA polymerase subunit ABC23, common to RNA polymerases I, II, and III × 1 (C4R1V1) RNA polymerase II subunit × 1 (C4R9A1) DNA-directed RNA polymerases I, II, and III subunit RPABC3 × 1 (C4R273) DNA-directed RNA polymerase subunit × 1 (F2QPE6) RNA polymerase subunit ABC10-beta, common to RNA polymerases I, II, and III × 1 (C4R009) RNA polymerase II subunit B12.5 × 1 (C4R3Z5) RNA polymerase subunit ABC10-alpha × 1 (F2QMI1) DNA (198-MER) × 1 ;RNA (5'-R(P*CP*CP*CP*GP*GP*UP*GP*UP*CP*UP*UP*GP*GP*GP*UP*G)-3') ; × 1 DNA (198-MER) × 1 Transcription elongation factor SPT4 × 1 (F2QTA2) Transcription elongation factor SPT5 × 1 (C4R370) Histone H3.3 × 2 (P84243) Histone H4 × 2 (P62805) Histone H2A-Bbd type 2/3 × 1 (P0C5Z0) Histone H2B type 1-J × 1 (P06899) ZN ZINC ION × 10 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES-KOH(pH7.5), 200 nM Zinc acetate, 0.1 mM TCEP-HCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

22 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C4QZ45_KOMPG
Isoform
PDB entities 13
Chains and sequence ranges Author chain M; PDBConstruct 1–110; UniProt 1–110

Transcription elongation factor SPT4

Komagataella phaffii

UniProt F2QTA2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 21 DNA 2 RNA 1 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain V; UniProt 1–114 Not recorded DNA-directed RNA polymerase subunit × 1 (C4R4Y0) DNA-directed RNA polymerase subunit beta × 1 (C4QZQ7) RNA polymerase II third largest subunit B44, part of central core × 1 (C4R7L2) RNA polymerase II subunit B32 × 1 (C4R2U9) DNA-directed RNA polymerases I, II, and III subunit RPABC1 × 1 (C4R3P8) RNA polymerase subunit ABC23, common to RNA polymerases I, II, and III × 1 (C4R1V1) RNA polymerase II subunit × 1 (C4R9A1) DNA-directed RNA polymerases I, II, and III subunit RPABC3 × 1 (C4R273) DNA-directed RNA polymerase subunit × 1 (F2QPE6) RNA polymerase subunit ABC10-beta, common to RNA polymerases I, II, and III × 1 (C4R009) RNA polymerase II subunit B12.5 × 1 (C4R3Z5) RNA polymerase subunit ABC10-alpha × 1 (F2QMI1) Transcription elongation factor 1 homolog × 1 (C4QZ45) DNA (198-MER) × 1 ;RNA (5'-R(P*CP*CP*CP*GP*GP*UP*GP*UP*CP*UP*UP*GP*GP*GP*UP*G)-3') ; × 1 DNA (198-MER) × 1 Transcription elongation factor SPT5 × 1 (C4R370) Histone H3.3 × 2 (P84243) Histone H4 × 2 (P62805) Histone H2A-Bbd type 2/3 × 1 (P0C5Z0) Histone H2B type 1-J × 1 (P06899) ZN ZINC ION × 10 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES-KOH(pH7.5), 200 nM Zinc acetate, 0.1 mM TCEP-HCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name F2QTA2_KOMPC
Isoform
PDB entities 17
Chains and sequence ranges Author chain V; PDBConstruct 1–114; UniProt 1–114

Transcription elongation factor SPT5

Komagataella phaffii

UniProt C4R370

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 21 DNA 2 RNA 1 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain W; UniProt 1–908 Not recorded DNA-directed RNA polymerase subunit × 1 (C4R4Y0) DNA-directed RNA polymerase subunit beta × 1 (C4QZQ7) RNA polymerase II third largest subunit B44, part of central core × 1 (C4R7L2) RNA polymerase II subunit B32 × 1 (C4R2U9) DNA-directed RNA polymerases I, II, and III subunit RPABC1 × 1 (C4R3P8) RNA polymerase subunit ABC23, common to RNA polymerases I, II, and III × 1 (C4R1V1) RNA polymerase II subunit × 1 (C4R9A1) DNA-directed RNA polymerases I, II, and III subunit RPABC3 × 1 (C4R273) DNA-directed RNA polymerase subunit × 1 (F2QPE6) RNA polymerase subunit ABC10-beta, common to RNA polymerases I, II, and III × 1 (C4R009) RNA polymerase II subunit B12.5 × 1 (C4R3Z5) RNA polymerase subunit ABC10-alpha × 1 (F2QMI1) Transcription elongation factor 1 homolog × 1 (C4QZ45) DNA (198-MER) × 1 ;RNA (5'-R(P*CP*CP*CP*GP*GP*UP*GP*UP*CP*UP*UP*GP*GP*GP*UP*G)-3') ; × 1 DNA (198-MER) × 1 Transcription elongation factor SPT4 × 1 (F2QTA2) Histone H3.3 × 2 (P84243) Histone H4 × 2 (P62805) Histone H2A-Bbd type 2/3 × 1 (P0C5Z0) Histone H2B type 1-J × 1 (P06899) ZN ZINC ION × 10 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES-KOH(pH7.5), 200 nM Zinc acetate, 0.1 mM TCEP-HCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

23 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C4R370_KOMPG
Isoform
PDB entities 18
Chains and sequence ranges Author chain W; PDBConstruct 1–908; UniProt 1–908

Histone H3.3

Homo sapiens

UniProt P84243

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 21 DNA 2 RNA 1 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain a; UniProt 1–136 Chain e; UniProt 1–136 Not recorded DNA-directed RNA polymerase subunit × 1 (C4R4Y0) DNA-directed RNA polymerase subunit beta × 1 (C4QZQ7) RNA polymerase II third largest subunit B44, part of central core × 1 (C4R7L2) RNA polymerase II subunit B32 × 1 (C4R2U9) DNA-directed RNA polymerases I, II, and III subunit RPABC1 × 1 (C4R3P8) RNA polymerase subunit ABC23, common to RNA polymerases I, II, and III × 1 (C4R1V1) RNA polymerase II subunit × 1 (C4R9A1) DNA-directed RNA polymerases I, II, and III subunit RPABC3 × 1 (C4R273) DNA-directed RNA polymerase subunit × 1 (F2QPE6) RNA polymerase subunit ABC10-beta, common to RNA polymerases I, II, and III × 1 (C4R009) RNA polymerase II subunit B12.5 × 1 (C4R3Z5) RNA polymerase subunit ABC10-alpha × 1 (F2QMI1) Transcription elongation factor 1 homolog × 1 (C4QZ45) DNA (198-MER) × 1 ;RNA (5'-R(P*CP*CP*CP*GP*GP*UP*GP*UP*CP*UP*UP*GP*GP*GP*UP*G)-3') ; × 1 DNA (198-MER) × 1 Transcription elongation factor SPT4 × 1 (F2QTA2) Transcription elongation factor SPT5 × 1 (C4R370) Histone H4 × 2 (P62805) Histone H2A-Bbd type 2/3 × 1 (P0C5Z0) Histone H2B type 1-J × 1 (P06899) ZN ZINC ION × 10 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES-KOH(pH7.5), 200 nM Zinc acetate, 0.1 mM TCEP-HCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

94 other PDB entries and 123 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H33_HUMAN
Isoform
PDB entities 19
Chains and sequence ranges Author chain a; PDBConstruct 1–136; UniProt 1–136 Author chain e; 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 Other combination Heteromer Protein × 21 DNA 2 RNA 1 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain b; UniProt 1–103 Chain f; UniProt 1–103 Not recorded DNA-directed RNA polymerase subunit × 1 (C4R4Y0) DNA-directed RNA polymerase subunit beta × 1 (C4QZQ7) RNA polymerase II third largest subunit B44, part of central core × 1 (C4R7L2) RNA polymerase II subunit B32 × 1 (C4R2U9) DNA-directed RNA polymerases I, II, and III subunit RPABC1 × 1 (C4R3P8) RNA polymerase subunit ABC23, common to RNA polymerases I, II, and III × 1 (C4R1V1) RNA polymerase II subunit × 1 (C4R9A1) DNA-directed RNA polymerases I, II, and III subunit RPABC3 × 1 (C4R273) DNA-directed RNA polymerase subunit × 1 (F2QPE6) RNA polymerase subunit ABC10-beta, common to RNA polymerases I, II, and III × 1 (C4R009) RNA polymerase II subunit B12.5 × 1 (C4R3Z5) RNA polymerase subunit ABC10-alpha × 1 (F2QMI1) Transcription elongation factor 1 homolog × 1 (C4QZ45) DNA (198-MER) × 1 ;RNA (5'-R(P*CP*CP*CP*GP*GP*UP*GP*UP*CP*UP*UP*GP*GP*GP*UP*G)-3') ; × 1 DNA (198-MER) × 1 Transcription elongation factor SPT4 × 1 (F2QTA2) Transcription elongation factor SPT5 × 1 (C4R370) Histone H3.3 × 2 (P84243) Histone H2A-Bbd type 2/3 × 1 (P0C5Z0) Histone H2B type 1-J × 1 (P06899) ZN ZINC ION × 10 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES-KOH(pH7.5), 200 nM Zinc acetate, 0.1 mM TCEP-HCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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 20
Chains and sequence ranges Author chain b; PDBConstruct 1–103; UniProt 1–103 Author chain f; PDBConstruct 1–103; UniProt 1–103

Histone H2A-Bbd type 2/3

Homo sapiens

UniProt P0C5Z0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 21 DNA 2 RNA 1 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain c; UniProt 1–115 Not recorded DNA-directed RNA polymerase subunit × 1 (C4R4Y0) DNA-directed RNA polymerase subunit beta × 1 (C4QZQ7) RNA polymerase II third largest subunit B44, part of central core × 1 (C4R7L2) RNA polymerase II subunit B32 × 1 (C4R2U9) DNA-directed RNA polymerases I, II, and III subunit RPABC1 × 1 (C4R3P8) RNA polymerase subunit ABC23, common to RNA polymerases I, II, and III × 1 (C4R1V1) RNA polymerase II subunit × 1 (C4R9A1) DNA-directed RNA polymerases I, II, and III subunit RPABC3 × 1 (C4R273) DNA-directed RNA polymerase subunit × 1 (F2QPE6) RNA polymerase subunit ABC10-beta, common to RNA polymerases I, II, and III × 1 (C4R009) RNA polymerase II subunit B12.5 × 1 (C4R3Z5) RNA polymerase subunit ABC10-alpha × 1 (F2QMI1) Transcription elongation factor 1 homolog × 1 (C4QZ45) DNA (198-MER) × 1 ;RNA (5'-R(P*CP*CP*CP*GP*GP*UP*GP*UP*CP*UP*UP*GP*GP*GP*UP*G)-3') ; × 1 DNA (198-MER) × 1 Transcription elongation factor SPT4 × 1 (F2QTA2) Transcription elongation factor SPT5 × 1 (C4R370) Histone H3.3 × 2 (P84243) Histone H4 × 2 (P62805) Histone H2B type 1-J × 1 (P06899) ZN ZINC ION × 10 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES-KOH(pH7.5), 200 nM Zinc acetate, 0.1 mM TCEP-HCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2AB2_HUMAN
Isoform
PDB entities 21
Chains and sequence ranges Author chain c; PDBConstruct 1–115; UniProt 1–115

Histone H2B type 1-J

Homo sapiens

UniProt P06899

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 21 DNA 2 RNA 1 PDB declaration: 24-meric(24) Consistent with all polymer counts Chain d; UniProt 1–126 Not recorded DNA-directed RNA polymerase subunit × 1 (C4R4Y0) DNA-directed RNA polymerase subunit beta × 1 (C4QZQ7) RNA polymerase II third largest subunit B44, part of central core × 1 (C4R7L2) RNA polymerase II subunit B32 × 1 (C4R2U9) DNA-directed RNA polymerases I, II, and III subunit RPABC1 × 1 (C4R3P8) RNA polymerase subunit ABC23, common to RNA polymerases I, II, and III × 1 (C4R1V1) RNA polymerase II subunit × 1 (C4R9A1) DNA-directed RNA polymerases I, II, and III subunit RPABC3 × 1 (C4R273) DNA-directed RNA polymerase subunit × 1 (F2QPE6) RNA polymerase subunit ABC10-beta, common to RNA polymerases I, II, and III × 1 (C4R009) RNA polymerase II subunit B12.5 × 1 (C4R3Z5) RNA polymerase subunit ABC10-alpha × 1 (F2QMI1) Transcription elongation factor 1 homolog × 1 (C4QZ45) DNA (198-MER) × 1 ;RNA (5'-R(P*CP*CP*CP*GP*GP*UP*GP*UP*CP*UP*UP*GP*GP*GP*UP*G)-3') ; × 1 DNA (198-MER) × 1 Transcription elongation factor SPT4 × 1 (F2QTA2) Transcription elongation factor SPT5 × 1 (C4R370) Histone H3.3 × 2 (P84243) Histone H4 × 2 (P62805) Histone H2A-Bbd type 2/3 × 1 (P0C5Z0) ZN ZINC ION × 10 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES-KOH(pH7.5), 200 nM Zinc acetate, 0.1 mM TCEP-HCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

290 other PDB entries and 301 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1J_HUMAN
Isoform
PDB entities 22
Chains and sequence ranges Author chain d; PDBConstruct 1–126; UniProt 1–126

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 9ii7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ii7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9ii7
Deposition date deposition_date2024-06-19
Structure title titleRNA polymerase II elongation complex stalled at SHL(-1) of the nucleosome containing histone variant H2A.B
Keywords keywordsTranscription-DNA-RNA COMPLEX, RNAPII, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier62.62
Radius of gyration Rg (electron density) rg_electron61.31
Forward intensity I(0) i06493970000.00
Molecular weight molecular_weight626790.0 kDa
Excluded volume excluded_volume762900 ų
Envelope volume envelope_volume1189200 ų
Hydration-shell volume shell_volume158830 ų
Envelope diameter envelope_diameter226.9
Shell Rg shell_rg66.23
Envelope Rg envelope_rg60.32
Shape Rg shape_rg61.26
Total Rg total_rg61.56
Total atoms total_atoms43686
Residues n_residues5109
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 dmax200.2
Rg (real space) rg_real62.58
Rg uncertainty (real space) rg_real_error1.10
I(0) (real space) i0_real6.4880e+09
I(0) uncertainty (real space) i0_real_error1.2120e+08
Rg (reciprocal space) rg_reciprocal62.53
I(0) (reciprocal space) i0_reciprocal6492000000.0000
Solution quality estimate total_estimate0.6246
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary72.1
Skewness Skewness skewness0.462
Kurtosis Kurtosis kurtosis-0.028
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0054
Highest regularization parameter α highest_alpha755000000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.871; Stabil: 1.000; Sysdev: 0.004; Positv: 1.000; Valcen: 0.967; Smooth: 0.523

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (24)

8. Citations (1)

9. Files and Curves (10)