MolNFT v1 · #190771 · protein + DNA
Structure of the human ccan cenp-a alpha-satellite complex
7YWX: “Structure of the human ccan cenp-a alpha-satellite complex”. Electron microscopy. MolNFT v1 #190771 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7YWX
- Type
- protein + DNA
- Length
- 4,264 residues
- Chains
- 27
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9H3R5, Q92674, Q9BS16, Q8N0S6, Q9NSP4, Q96H22, Q9BU64, Q7L2Z9, Q71F23, Q6IPU0, Q13352, Q96BT3, Q5EE01, Q8N2Z9, A8MT69, P49450, P62805, Q93077, P62807, Q03188
Structure
electron microscopy · 26 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| H | — | protein | 204 | — | Q9H3R5 |
| I | — | protein | 622 | — | Q92674 |
| K | — | protein | 233 | — | Q9BS16 |
| L | — | protein | 312 | — | Q8N0S6 |
| M | — | protein | 172 | — | Q9NSP4 |
| N | — | protein | 318 | — | Q96H22 |
| O | — | protein | 210 | — | Q9BU64 |
| Q | — | protein | 191 | — | Q7L2Z9 |
| U | — | protein | 166 | — | Q71F23 |
| P | — | protein | 224 | — | Q6IPU0 |
| R | — | protein | 80 | — | Q13352 |
| T | — | protein | 112 | — | Q96BT3 |
| W | — | protein | 88 | — | Q5EE01 |
| S | — | protein | 120 | — | Q8N2Z9 |
| X | — | protein | 74 | — | A8MT69 |
| i | — | dna | 162 | — | — |
| J | — | dna | 162 | — | — |
| A | — | protein | 99 | — | P49450 |
| B | — | protein | 78 | — | P62805 |
| C | — | protein | 98 | — | Q93077 |
| D, V | — | protein | 92 | — | P62807 |
| E | — | protein | 94 | — | P49450 |
| F | — | protein | 80 | — | P62805 |
| G | — | protein | 103 | — | Q93077 |
| a | — | protein | 21 | — | Q03188 |
| b | — | protein | 57 | — | Q03188 |
Compared structures
- 7YWX · Structure of the human CCAN CENP-A alpha-satellite complex · the same entry in another collection · chain L against L, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9H3R5
- Every structure of UniProt Q92674
- Every structure of UniProt Q9BS16
- Every structure of UniProt Q8N0S6
- Every structure of UniProt Q9NSP4
- Every structure of UniProt Q96H22
- Every structure of UniProt Q9BU64
- Every structure of UniProt Q7L2Z9
- Every structure of UniProt Q71F23
- Every structure of UniProt Q6IPU0
- Every structure of UniProt Q13352
- Every structure of UniProt Q96BT3
- Every structure of UniProt Q5EE01
- Every structure of UniProt Q8N2Z9
- Every structure of UniProt A8MT69
- Every structure of UniProt P49450
- Every structure of UniProt P62805
- Every structure of UniProt Q93077
- Every structure of UniProt P62807
- Every structure of UniProt Q03188
- Elsewhere: RCSB PDB 7YWX · PDBe 7YWX · UniProt Q9H3R5 · UniProt Q92674 · UniProt Q9BS16 · UniProt Q8N0S6 · UniProt Q9NSP4 · UniProt Q96H22 · UniProt Q9BU64 · UniProt Q7L2Z9 · UniProt Q71F23 · UniProt Q6IPU0 · UniProt Q13352 · UniProt Q96BT3 · UniProt Q5EE01 · UniProt Q8N2Z9 · UniProt A8MT69 · UniProt P49450 · UniProt P62805 · UniProt Q93077 · UniProt P62807 · UniProt Q03188
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