Research workbench
Model of human anaphase-promoting COMPLEX/CYCLOSOME (APC/C-CDH1) with E2 UBE2S poised for polyubiquitination where UBE2S, APC2, and APC11 are modeled into low resolution density
Analyse Model of human anaphase-promoting COMPLEX/CYCLOSOME (APC/C-CDH1) with E2 UBE2S… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5L9T
- Type
- protein
- Length
- 8,038 residues
- Chains
- 22
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anaphase-promoting complex subunit 1; Anaphase-promoting complex subunit 11; Cell…
- EC
- 2.7.11.1, 2.3.2.23
- UniProt
- Q9H1A4, Q9NYG5, Q9UJX2, P60006, Q96DE5, P30260, Q8NHZ8, Q9UJX5, Q13042, Q9UM13, Q9BS18, Q9UJX6, Q9UJX4, Q9UM11, P0CG47, P34244, Q16763, Q9UJX3
- Pockets
- 7 · best druggability 0.43
Structure
electron microscopy · 21 distinct chains · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Anaphase-promoting complex subunit 1 | protein | 1380 | 0% helix, 0% strand | Q9H1A4 |
| B | Anaphase-promoting complex subunit 11 | protein | 68 | 0% helix, 0% strand | Q9NYG5 |
| C | Cell division cycle protein 23 homolog | protein | 475 | 0% helix, 0% strand | Q9UJX2 |
| D | Anaphase-promoting complex subunit 15 | protein | 55 | 0% helix, 0% strand | P60006 |
| E | Anaphase-promoting complex subunit 16 | protein | 56 | 0% helix, 0% strand | Q96DE5 |
| F | Cell division cycle protein 27 homolog | protein | 482 | 0% helix, 0% strand | P30260 |
| G, W | Anaphase-promoting complex subunit CDC26 | protein | 25 | 0% helix, 0% strand | Q8NHZ8 |
| H | Cell division cycle protein 27 homolog | protein | 483 | 0% helix, 0% strand | P30260 |
| I | Anaphase-promoting complex subunit 4 | protein | 727 | 0% helix, 0% strand | Q9UJX5 |
| J | Cell division cycle protein 16 homolog | protein | 504 | 0% helix, 0% strand | Q13042 |
| K | Cell division cycle protein 16 homolog | protein | 493 | 0% helix, 0% strand | Q13042 |
| L | Anaphase-promoting complex subunit 10 | protein | 170 | 0% helix, 0% strand | Q9UM13 |
| M | Anaphase-promoting complex subunit 13 | protein | 42 | 0% helix, 0% strand | Q9BS18 |
| N | Anaphase-promoting complex subunit 2 | protein | 546 | 0% helix, 0% strand | Q9UJX6 |
| O | Anaphase-promoting complex subunit 5 | protein | 685 | 0% helix, 0% strand | Q9UJX4 |
| P | Cell division cycle protein 23 homolog | protein | 443 | 0% helix, 0% strand | Q9UJX2 |
| R | Fizzy-related protein homolog | protein | 385 | 0% helix, 0% strand | Q9UM11 |
| S | UBIQUITIN_VARIANT-HSL1(SUBSTRATE) fusion (EC 2.7.11.1) | protein | 84 | 0% helix, 0% strand | P0CG47, P34244 |
| T | Ubiquitin-conjugating enzyme E2 S (EC 2.3.2.23) | protein | 97 | 0% helix, 0% strand | Q16763 |
| X | Anaphase-promoting complex subunit 7 | protein | 397 | 0% helix, 0% strand | Q9UJX3 |
| Y | Anaphase-promoting complex subunit 7 | protein | 416 | 0% helix, 0% strand | Q9UJX3 |
Pockets
7 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 149 | 0.43 | 0.73 | 36 | empty |
| 2 | 106 | 0.38 | 0.73 | 30 | empty |
| 3 | 76 | 0.33 | 0.73 | 22 | empty |
| 4 | 70 | 0.32 | 0.73 | 24 | empty |
| 5 | 60 | 0.29 | 0.72 | 19 | empty |
Interfaces
37 interfaces between chains.
- A–O · 410 Ų buried · 0 hydrogen bonds · protein-protein
- B–N · 332 Ų buried · 0 hydrogen bonds · protein-protein
- I–O · 215 Ų buried · 0 hydrogen bonds · protein-protein
- X–Y · 176 Ų buried · 0 hydrogen bonds · protein-protein
- A–L · 164 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 5L9T · Model of human Anaphase-promoting complex/Cyclosome (APC/C-CDH1) with E2 UBE2S poised for… · the same entry in another collection · chain K against K, 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 Q9H1A4
- Every structure of UniProt Q9NYG5
- Every structure of UniProt Q9UJX2
- Every structure of UniProt P60006
- Every structure of UniProt Q96DE5
- Every structure of UniProt P30260
- Every structure of UniProt Q8NHZ8
- Every structure of UniProt Q9UJX5
- Every structure of UniProt Q13042
- Every structure of UniProt Q9UM13
- Every structure of UniProt Q9BS18
- Every structure of UniProt Q9UJX6
- Every structure of UniProt Q9UJX4
- Every structure of UniProt Q9UM11
- Every structure of UniProt P0CG47
- Every structure of UniProt P34244
- Every structure of UniProt Q16763
- Every structure of UniProt Q9UJX3
- Elsewhere: RCSB PDB 5L9T · PDBe 5L9T · UniProt Q9H1A4 · UniProt Q9NYG5 · UniProt Q9UJX2 · UniProt P60006 · UniProt Q96DE5 · UniProt P30260 · UniProt Q8NHZ8 · UniProt Q9UJX5 · UniProt Q13042 · UniProt Q9UM13 · UniProt Q9BS18 · UniProt Q9UJX6 · UniProt Q9UJX4 · UniProt Q9UM11 · UniProt P0CG47 · UniProt P34244 · UniProt Q16763 · UniProt Q9UJX3
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