7yyh

Structure of the human CCANdeltaT CENP-A alpha-satellite complex

Method: ELECTRON MICROSCOPY Dmax: 228.7 Å Quality: GOOD

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

Histone H3-like centromeric protein A

Homo sapiens

UniProt P49450

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 × 21 DNA 2 PDB declaration: 23-meric(23) Consistent with all polymer counts Chain A; UniProt 1–140 Chain E; UniProt 1–140 Not recorded Histone H4 × 2 (P62805) Histone H2A type 1-C × 2 (Q93077) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Centromere protein H × 1 (Q9H3R5) Centromere protein I × 1 (Q92674) DNA (171-MER) × 1 Centromere protein K × 1 (Q9BS16) Centromere protein L × 1 (Q8N0S6) Centromere protein M × 1 (Q9NSP4) Centromere protein N × 1 (Q96H22) Centromere protein O × 1 (Q9BU64) Centromere protein P × 1 (Q6IPU0) Centromere protein Q × 1 (Q7L2Z9) Centromere protein R × 1 (Q13352) Centromere protein U × 1 (Q71F23) Centromere protein C × 2 (Q03188) DNA (171-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.90 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.

33 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CENPA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–140; UniProt 1–140 Author chain E; PDBConstruct 1–140; UniProt 1–140

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 × 21 DNA 2 PDB declaration: 23-meric(23) Consistent with all polymer counts Chain B; UniProt 1–103 Chain F; UniProt 1–103 Not recorded Histone H3-like centromeric protein A × 2 (P49450) Histone H2A type 1-C × 2 (Q93077) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Centromere protein H × 1 (Q9H3R5) Centromere protein I × 1 (Q92674) DNA (171-MER) × 1 Centromere protein K × 1 (Q9BS16) Centromere protein L × 1 (Q8N0S6) Centromere protein M × 1 (Q9NSP4) Centromere protein N × 1 (Q96H22) Centromere protein O × 1 (Q9BU64) Centromere protein P × 1 (Q6IPU0) Centromere protein Q × 1 (Q7L2Z9) Centromere protein R × 1 (Q13352) Centromere protein U × 1 (Q71F23) Centromere protein C × 2 (Q03188) DNA (171-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.90 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–103; UniProt 1–103 Author chain F; PDBConstruct 1–103; UniProt 1–103

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 × 21 DNA 2 PDB declaration: 23-meric(23) Consistent with all polymer counts Chain C; UniProt 1–130 Chain G; UniProt 1–130 Not recorded Histone H3-like centromeric protein A × 2 (P49450) Histone H4 × 2 (P62805) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Centromere protein H × 1 (Q9H3R5) Centromere protein I × 1 (Q92674) DNA (171-MER) × 1 Centromere protein K × 1 (Q9BS16) Centromere protein L × 1 (Q8N0S6) Centromere protein M × 1 (Q9NSP4) Centromere protein N × 1 (Q96H22) Centromere protein O × 1 (Q9BU64) Centromere protein P × 1 (Q6IPU0) Centromere protein Q × 1 (Q7L2Z9) Centromere protein R × 1 (Q13352) Centromere protein U × 1 (Q71F23) Centromere protein C × 2 (Q03188) DNA (171-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.90 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 3
Chains and sequence ranges Author chain C; PDBConstruct 1–130; UniProt 1–130 Author chain G; 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 × 21 DNA 2 PDB declaration: 23-meric(23) Consistent with all polymer counts Chain D; UniProt 1–126 Chain h; UniProt 1–126 Not recorded Histone H3-like centromeric protein A × 2 (P49450) Histone H4 × 2 (P62805) Histone H2A type 1-C × 2 (Q93077) Centromere protein H × 1 (Q9H3R5) Centromere protein I × 1 (Q92674) DNA (171-MER) × 1 Centromere protein K × 1 (Q9BS16) Centromere protein L × 1 (Q8N0S6) Centromere protein M × 1 (Q9NSP4) Centromere protein N × 1 (Q96H22) Centromere protein O × 1 (Q9BU64) Centromere protein P × 1 (Q6IPU0) Centromere protein Q × 1 (Q7L2Z9) Centromere protein R × 1 (Q13352) Centromere protein U × 1 (Q71F23) Centromere protein C × 2 (Q03188) DNA (171-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.90 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 4
Chains and sequence ranges Author chain D; PDBConstruct 1–126; UniProt 1–126 Author chain h; PDBConstruct 1–126; UniProt 1–126

Centromere protein H

Homo sapiens

UniProt Q9H3R5

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 × 21 DNA 2 PDB declaration: 23-meric(23) Consistent with all polymer counts Chain H; UniProt 1–247 Not recorded Histone H3-like centromeric protein A × 2 (P49450) Histone H4 × 2 (P62805) Histone H2A type 1-C × 2 (Q93077) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Centromere protein I × 1 (Q92674) DNA (171-MER) × 1 Centromere protein K × 1 (Q9BS16) Centromere protein L × 1 (Q8N0S6) Centromere protein M × 1 (Q9NSP4) Centromere protein N × 1 (Q96H22) Centromere protein O × 1 (Q9BU64) Centromere protein P × 1 (Q6IPU0) Centromere protein Q × 1 (Q7L2Z9) Centromere protein R × 1 (Q13352) Centromere protein U × 1 (Q71F23) Centromere protein C × 2 (Q03188) DNA (171-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.90 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 CENPH_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain H; PDBConstruct 1–247; UniProt 1–247

Centromere protein I

Homo sapiens

UniProt Q92674

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 × 21 DNA 2 PDB declaration: 23-meric(23) Consistent with all polymer counts Chain I; UniProt 1–756 Not recorded Histone H3-like centromeric protein A × 2 (P49450) Histone H4 × 2 (P62805) Histone H2A type 1-C × 2 (Q93077) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Centromere protein H × 1 (Q9H3R5) DNA (171-MER) × 1 Centromere protein K × 1 (Q9BS16) Centromere protein L × 1 (Q8N0S6) Centromere protein M × 1 (Q9NSP4) Centromere protein N × 1 (Q96H22) Centromere protein O × 1 (Q9BU64) Centromere protein P × 1 (Q6IPU0) Centromere protein Q × 1 (Q7L2Z9) Centromere protein R × 1 (Q13352) Centromere protein U × 1 (Q71F23) Centromere protein C × 2 (Q03188) DNA (171-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.90 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.

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CENPI_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain I; PDBConstruct 1–756; UniProt 1–756

Centromere protein K

Homo sapiens

UniProt Q9BS16

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 × 21 DNA 2 PDB declaration: 23-meric(23) Consistent with all polymer counts Chain K; UniProt 1–269 Not recorded Histone H3-like centromeric protein A × 2 (P49450) Histone H4 × 2 (P62805) Histone H2A type 1-C × 2 (Q93077) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Centromere protein H × 1 (Q9H3R5) Centromere protein I × 1 (Q92674) DNA (171-MER) × 1 Centromere protein L × 1 (Q8N0S6) Centromere protein M × 1 (Q9NSP4) Centromere protein N × 1 (Q96H22) Centromere protein O × 1 (Q9BU64) Centromere protein P × 1 (Q6IPU0) Centromere protein Q × 1 (Q7L2Z9) Centromere protein R × 1 (Q13352) Centromere protein U × 1 (Q71F23) Centromere protein C × 2 (Q03188) DNA (171-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.90 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 CENPK_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain K; PDBConstruct 1–269; UniProt 1–269

Centromere protein L

Homo sapiens

UniProt Q8N0S6

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 × 21 DNA 2 PDB declaration: 23-meric(23) Consistent with all polymer counts Chain L; UniProt 1–344 Not recorded Histone H3-like centromeric protein A × 2 (P49450) Histone H4 × 2 (P62805) Histone H2A type 1-C × 2 (Q93077) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Centromere protein H × 1 (Q9H3R5) Centromere protein I × 1 (Q92674) DNA (171-MER) × 1 Centromere protein K × 1 (Q9BS16) Centromere protein M × 1 (Q9NSP4) Centromere protein N × 1 (Q96H22) Centromere protein O × 1 (Q9BU64) Centromere protein P × 1 (Q6IPU0) Centromere protein Q × 1 (Q7L2Z9) Centromere protein R × 1 (Q13352) Centromere protein U × 1 (Q71F23) Centromere protein C × 2 (Q03188) DNA (171-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.90 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.

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CENPL_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain L; PDBConstruct 1–344; UniProt 1–344

Centromere protein M

Homo sapiens

UniProt Q9NSP4

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 × 21 DNA 2 PDB declaration: 23-meric(23) Consistent with all polymer counts Chain M; UniProt 1–180 Not recorded Histone H3-like centromeric protein A × 2 (P49450) Histone H4 × 2 (P62805) Histone H2A type 1-C × 2 (Q93077) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Centromere protein H × 1 (Q9H3R5) Centromere protein I × 1 (Q92674) DNA (171-MER) × 1 Centromere protein K × 1 (Q9BS16) Centromere protein L × 1 (Q8N0S6) Centromere protein N × 1 (Q96H22) Centromere protein O × 1 (Q9BU64) Centromere protein P × 1 (Q6IPU0) Centromere protein Q × 1 (Q7L2Z9) Centromere protein R × 1 (Q13352) Centromere protein U × 1 (Q71F23) Centromere protein C × 2 (Q03188) DNA (171-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.90 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.

13 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CENPM_HUMAN
Isoform
PDB entities 10
Chains and sequence ranges Author chain M; PDBConstruct 1–180; UniProt 1–180

Centromere protein N

Homo sapiens

UniProt Q96H22

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 × 21 DNA 2 PDB declaration: 23-meric(23) Consistent with all polymer counts Chain N; UniProt 1–339 Not recorded Histone H3-like centromeric protein A × 2 (P49450) Histone H4 × 2 (P62805) Histone H2A type 1-C × 2 (Q93077) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Centromere protein H × 1 (Q9H3R5) Centromere protein I × 1 (Q92674) DNA (171-MER) × 1 Centromere protein K × 1 (Q9BS16) Centromere protein L × 1 (Q8N0S6) Centromere protein M × 1 (Q9NSP4) Centromere protein O × 1 (Q9BU64) Centromere protein P × 1 (Q6IPU0) Centromere protein Q × 1 (Q7L2Z9) Centromere protein R × 1 (Q13352) Centromere protein U × 1 (Q71F23) Centromere protein C × 2 (Q03188) DNA (171-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.90 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.

19 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CENPN_HUMAN
Isoform
PDB entities 11
Chains and sequence ranges Author chain N; PDBConstruct 1–339; UniProt 1–339

Centromere protein O

Homo sapiens

UniProt Q9BU64

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 × 21 DNA 2 PDB declaration: 23-meric(23) Consistent with all polymer counts Chain O; UniProt 1–300 Not recorded Histone H3-like centromeric protein A × 2 (P49450) Histone H4 × 2 (P62805) Histone H2A type 1-C × 2 (Q93077) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Centromere protein H × 1 (Q9H3R5) Centromere protein I × 1 (Q92674) DNA (171-MER) × 1 Centromere protein K × 1 (Q9BS16) Centromere protein L × 1 (Q8N0S6) Centromere protein M × 1 (Q9NSP4) Centromere protein N × 1 (Q96H22) Centromere protein P × 1 (Q6IPU0) Centromere protein Q × 1 (Q7L2Z9) Centromere protein R × 1 (Q13352) Centromere protein U × 1 (Q71F23) Centromere protein C × 2 (Q03188) DNA (171-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.90 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 CENPO_HUMAN
Isoform
PDB entities 12
Chains and sequence ranges Author chain O; PDBConstruct 1–300; UniProt 1–300

Centromere protein P

Homo sapiens

UniProt Q6IPU0

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 × 21 DNA 2 PDB declaration: 23-meric(23) Consistent with all polymer counts Chain P; UniProt 1–288 Not recorded Histone H3-like centromeric protein A × 2 (P49450) Histone H4 × 2 (P62805) Histone H2A type 1-C × 2 (Q93077) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Centromere protein H × 1 (Q9H3R5) Centromere protein I × 1 (Q92674) DNA (171-MER) × 1 Centromere protein K × 1 (Q9BS16) Centromere protein L × 1 (Q8N0S6) Centromere protein M × 1 (Q9NSP4) Centromere protein N × 1 (Q96H22) Centromere protein O × 1 (Q9BU64) Centromere protein Q × 1 (Q7L2Z9) Centromere protein R × 1 (Q13352) Centromere protein U × 1 (Q71F23) Centromere protein C × 2 (Q03188) DNA (171-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.90 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 CENPP_HUMAN
Isoform
PDB entities 13
Chains and sequence ranges Author chain P; PDBConstruct 1–288; UniProt 1–288

Centromere protein Q

Homo sapiens

UniProt Q7L2Z9

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 × 21 DNA 2 PDB declaration: 23-meric(23) Consistent with all polymer counts Chain Q; UniProt 1–268 Not recorded Histone H3-like centromeric protein A × 2 (P49450) Histone H4 × 2 (P62805) Histone H2A type 1-C × 2 (Q93077) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Centromere protein H × 1 (Q9H3R5) Centromere protein I × 1 (Q92674) DNA (171-MER) × 1 Centromere protein K × 1 (Q9BS16) Centromere protein L × 1 (Q8N0S6) Centromere protein M × 1 (Q9NSP4) Centromere protein N × 1 (Q96H22) Centromere protein O × 1 (Q9BU64) Centromere protein P × 1 (Q6IPU0) Centromere protein R × 1 (Q13352) Centromere protein U × 1 (Q71F23) Centromere protein C × 2 (Q03188) DNA (171-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.90 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 CENPQ_HUMAN
Isoform
PDB entities 14
Chains and sequence ranges Author chain Q; PDBConstruct 1–268; UniProt 1–268

Centromere protein R

Homo sapiens

UniProt Q13352

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 × 21 DNA 2 PDB declaration: 23-meric(23) Consistent with all polymer counts Chain R; UniProt 1–177 Not recorded Histone H3-like centromeric protein A × 2 (P49450) Histone H4 × 2 (P62805) Histone H2A type 1-C × 2 (Q93077) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Centromere protein H × 1 (Q9H3R5) Centromere protein I × 1 (Q92674) DNA (171-MER) × 1 Centromere protein K × 1 (Q9BS16) Centromere protein L × 1 (Q8N0S6) Centromere protein M × 1 (Q9NSP4) Centromere protein N × 1 (Q96H22) Centromere protein O × 1 (Q9BU64) Centromere protein P × 1 (Q6IPU0) Centromere protein Q × 1 (Q7L2Z9) Centromere protein U × 1 (Q71F23) Centromere protein C × 2 (Q03188) DNA (171-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.90 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 CENPR_HUMAN
Isoform
PDB entities 15
Chains and sequence ranges Author chain R; PDBConstruct 1–177; UniProt 1–177

Centromere protein U

Homo sapiens

UniProt Q71F23

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 × 21 DNA 2 PDB declaration: 23-meric(23) Consistent with all polymer counts Chain U; UniProt 1–418 Not recorded Histone H3-like centromeric protein A × 2 (P49450) Histone H4 × 2 (P62805) Histone H2A type 1-C × 2 (Q93077) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Centromere protein H × 1 (Q9H3R5) Centromere protein I × 1 (Q92674) DNA (171-MER) × 1 Centromere protein K × 1 (Q9BS16) Centromere protein L × 1 (Q8N0S6) Centromere protein M × 1 (Q9NSP4) Centromere protein N × 1 (Q96H22) Centromere protein O × 1 (Q9BU64) Centromere protein P × 1 (Q6IPU0) Centromere protein Q × 1 (Q7L2Z9) Centromere protein R × 1 (Q13352) Centromere protein C × 2 (Q03188) DNA (171-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.90 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 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CENPU_HUMAN
Isoform
PDB entities 16
Chains and sequence ranges Author chain U; PDBConstruct 1–418; UniProt 1–418

Centromere protein C

Homo sapiens

UniProt Q03188

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 × 21 DNA 2 PDB declaration: 23-meric(23) Consistent with all polymer counts Chain k; UniProt 1–544 Chain l; UniProt 1–544 Not recorded Histone H3-like centromeric protein A × 2 (P49450) Histone H4 × 2 (P62805) Histone H2A type 1-C × 2 (Q93077) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Centromere protein H × 1 (Q9H3R5) Centromere protein I × 1 (Q92674) DNA (171-MER) × 1 Centromere protein K × 1 (Q9BS16) Centromere protein L × 1 (Q8N0S6) Centromere protein M × 1 (Q9NSP4) Centromere protein N × 1 (Q96H22) Centromere protein O × 1 (Q9BU64) Centromere protein P × 1 (Q6IPU0) Centromere protein Q × 1 (Q7L2Z9) Centromere protein R × 1 (Q13352) Centromere protein U × 1 (Q71F23) DNA (171-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.90 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 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CENPC_HUMAN
Isoform
PDB entities 17
Chains and sequence ranges Author chain k; PDBConstruct 1–544; UniProt 1–544 Author chain l; PDBConstruct 1–544; UniProt 1–544

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 7yyh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7yyh
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7yyh
Deposition date deposition_date2022-02-17
Structure title titleStructure of the human CCANdeltaT CENP-A alpha-satellite complex
Keywords keywordsChromosome, kinetochore, cell division, centromere, CELL CYCLE; CELL CYCLE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier69.84
Radius of gyration Rg (electron density) rg_electron69.37
Forward intensity I(0) i03931200000.00
Molecular weight molecular_weight479310.0 kDa
Excluded volume excluded_volume579150 ų
Envelope volume envelope_volume949920 ų
Hydration-shell volume shell_volume116660 ų
Envelope diameter envelope_diameter214.0
Shell Rg shell_rg66.14
Envelope Rg envelope_rg66.88
Shape Rg shape_rg69.31
Total Rg total_rg69.50
Total atoms total_atoms33344
Residues n_residues3679
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 dmax228.7
Rg (real space) rg_real69.79
Rg uncertainty (real space) rg_real_error2.08
I(0) (real space) i0_real3.9310e+09
I(0) uncertainty (real space) i0_real_error8.3490e+07
Rg (reciprocal space) rg_reciprocal69.83
I(0) (reciprocal space) i0_reciprocal3931000000.0000
Solution quality estimate total_estimate0.8325
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary83.2
Skewness Skewness skewness0.154
Kurtosis Kurtosis kurtosis-0.764
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha218000000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.941; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (18)

8. Citations (1)

9. Files and Curves (10)