Research workbench
Cryo-EM structure of clamped S.CEREVISIAE condensin-DNA complex (form I)
Analyse Cryo-EM structure of clamped S.CEREVISIAE condensin-DNA complex (form I) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7Q2X
- Type
- protein + DNA
- Length
- 2,170 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Structural maintenance of chromosomes protein 2; Structural maintenance of chromosomes…
- UniProt
- P38989, Q12267, P38170, Q06156
- Ligands
- ADP, BEF, MG
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 6 distinct chains · 60% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Structural maintenance of chromosomes protein 2 | protein | 431 | 48% helix, 19% strand | P38989 |
| B | Structural maintenance of chromosomes protein 4 | protein | 388 | 36% helix, 24% strand | Q12267 |
| C | Condensin complex subunit 2 | protein | 285 | 54% helix, 5% strand | P38170 |
| D | Condensin complex subunit 1 | protein | 994 | 76% helix, 0% strand | Q06156 |
| F | DNA (36-mer) | dna | 36 | — | — |
| G | DNA (36-mer) | dna | 36 | — | — |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
- BEF · Beryllium trifluoride ion · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1172 | 0.86 | 0.87 | 112 | ADP, BEF, MG |
| 2 | 751 | 0.82 | 0.85 | 72 | empty |
| 3 | 1165 | 0.80 | 0.81 | 111 | empty |
| 4 | 509 | 0.75 | 0.83 | 65 | empty |
| 5 | 258 | 0.75 | 0.89 | 43 | ADP, BEF, MG |
Interfaces
14 interfaces between chains.
- C–D · 4836 Ų buried · 33 hydrogen bonds · protein-protein
- A–C · 2606 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 1555 Ų buried · 9 hydrogen bonds · protein-protein
- F–G · 1498 Ų buried · 75 hydrogen bonds · nucleic-nucleic
- A–B · 1394 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 7Q2X · Cryo-EM structure of clamped S.cerevisiae condensin-DNA complex (Form I) · the same entry in another collection · chain G against G, TM-score 1.00
- Q06156 · AlphaFold monomer V2.0 prediction for condensin complex subunit 1 (Q06156) · a predicted model of the same protein · chain D against A, TM-score 0.95
- Q12267 · AlphaFold monomer V2.0 prediction for structural maintenance of chromosomes protein 4… · a predicted model of the same protein · chain B against A, TM-score 0.93
- P38989 · AlphaFold monomer V2.0 prediction for structural maintenance of chromosomes protein 2… · a predicted model of the same protein · chain A against A, TM-score 0.75
- P38170 · AlphaFold monomer V2.0 prediction for condensin complex subunit 2 (P38170) · a predicted model of the same protein · chain C against A, TM-score 0.37
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 P38989
- Every structure of UniProt Q12267
- Every structure of UniProt P38170
- Every structure of UniProt Q06156
- Elsewhere: RCSB PDB 7Q2X · PDBe 7Q2X · UniProt P38989 · UniProt Q12267 · UniProt P38170 · UniProt Q06156
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