Research workbench
Composite structure of EC+EC
Analyse Composite structure of EC+EC in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MEI
- Type
- protein + DNA + RNA
- Length
- 8,462 residues
- Chains
- 30
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA (74-mer); DNA-directed RNA polymerase subunit; DNA-directed RNA polymerase subunit…
- EC
- 2.7.7.6
- UniProt
- A0A6A5Q1P2, A0A6A5Q4H2, A0A6A5Q0Z3, A0A6A5PTI6, A0A6A5Q456, A0A6L0ZRI7, A0A6A5Q270, A0A6A5Q8C2, A0A7I9EWC2, A0A6A5Q7Q6, A0A6A5Q7A1, A0A6A5PY05, P41895, A0A6A5PZ00
- Ligands
- ZN, MG
- Pockets
- 20 · best druggability 0.88
Structure
electron microscopy · 19 distinct chains · 30% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| N | DNA (74-mer) | dna | 74 | — | — |
| O | DNA (74-mer) | dna | 74 | — | — |
| a, A | DNA-directed RNA polymerase subunit (EC 2.7.7.6) | protein | 1425 | 38% helix, 13% strand | A0A6A5Q1P2 |
| b | DNA-directed RNA polymerase subunit beta (EC 2.7.7.6) | protein | 1160 | 28% helix, 21% strand | A0A6A5Q4H2 |
| c, C | DNA-directed RNA polymerase II subunit RPB3 | protein | 265 | 24% helix, 23% strand | A0A6A5Q0Z3 |
| d, D | DNA-directed RNA polymerase II subunit RPB4 | protein | 168 | 59% helix, 3% strand | A0A6A5PTI6 |
| e, E | DNA-directed RNA polymerases I, II, and III subunit RPABC1 | protein | 214 | 35% helix, 19% strand | A0A6A5Q456 |
| f, F | DNA-directed RNA polymerases I,II,AND III subunit RPABC2 | protein | 87 | 31% helix, 15% strand | A0A6L0ZRI7 |
| g, G | DNA-directed RNA polymerase II subunit RPB7 | protein | 171 | 9% helix, 37% strand | A0A6A5Q270 |
| h, H | DNA-directed RNA polymerases I, II, and III subunit RPABC3 | protein | 135 | 0% helix, 44% strand | A0A6A5Q8C2 |
| i, I | DNA-directed RNA polymerase II subunit RPB9 | protein | 114 | 3% helix, 26% strand | A0A7I9EWC2 |
| j, J | DNA-directed RNA polymerases II subunit RPABC5 | protein | 66 | 47% helix, 0% strand | A0A6A5Q7Q6 |
| k, K | DNA-directed RNA polymerase II subunit RPB11 | protein | 115 | 38% helix, 24% strand | A0A6A5Q7A1 |
| l, L | DNA-directed RNA polymerases II subunit RPABC4 | protein | 44 | 0% helix, 9% strand | A0A6A5PY05 |
| r | RNA (5'- R(P*AP*AP*CP*UP*AP*GP*UP*UP*AP*AP*GP*AP*GP*GP*UP*U)-3') | rna | 16 | — | — |
| B | DNA-directed RNA polymerase subunit beta (EC 2.7.7.6) | protein | 1166 | 27% helix, 20% strand | A0A6A5Q4H2 |
| R | RNA (5'-R(P*UP*CP*GP*AP*GP*AP*GP*GP*AP*UP*CP*CP*CP*AP*A)- 3') | rna | 15 | — | — |
| Q | Transcription initiation factor iif subunit alpha | protein | 214 | 31% helix, 21% strand | P41895 |
| M | Transcription initiation factor iif subunit beta | protein | 135 | 16% helix, 39% strand | A0A6A5PZ00 |
Ligands and binding sites
- ZN · Zinc ion · metal · 16 copies · chains a, b, c, i, j, l, A, B, D, C, I, J, L
- MG · Magnesium ion · metal · 4 copies · chains a, r, A, R
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1012 | 0.88 | 0.90 | 126 | empty |
| 2 | 1023 | 0.88 | 0.89 | 105 | empty |
| 3 | 756 | 0.87 | 0.90 | 79 | empty |
| 4 | 1085 | 0.86 | 0.87 | 118 | empty |
| 5 | 965 | 0.85 | 0.86 | 119 | MG |
Interfaces
79 interfaces between chains.
- A–B · 9047 Ų buried · 95 hydrogen bonds · protein-protein
- a–b · 8881 Ų buried · 83 hydrogen bonds · protein-protein
- Q–M · 3160 Ų buried · 67 hydrogen bonds · protein-protein
- B–Q · 2334 Ų buried · 24 hydrogen bonds · protein-protein
- N–O · 2305 Ų buried · 182 hydrogen bonds · nucleic-nucleic
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 7MEI · Composite structure of EC+EC · the same entry in another collection · chain N against N, 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 A0A6A5Q1P2
- Every structure of UniProt A0A6A5Q4H2
- Every structure of UniProt A0A6A5Q0Z3
- Every structure of UniProt A0A6A5PTI6
- Every structure of UniProt A0A6A5Q456
- Every structure of UniProt A0A6L0ZRI7
- Every structure of UniProt A0A6A5Q270
- Every structure of UniProt A0A6A5Q8C2
- Every structure of UniProt A0A7I9EWC2
- Every structure of UniProt A0A6A5Q7Q6
- Every structure of UniProt A0A6A5Q7A1
- Every structure of UniProt A0A6A5PY05
- Every structure of UniProt P41895
- Every structure of UniProt A0A6A5PZ00
- Elsewhere: RCSB PDB 7MEI · PDBe 7MEI · UniProt A0A6A5Q1P2 · UniProt A0A6A5Q4H2 · UniProt A0A6A5Q0Z3 · UniProt A0A6A5PTI6 · UniProt A0A6A5Q456 · UniProt A0A6L0ZRI7 · UniProt A0A6A5Q270 · UniProt A0A6A5Q8C2 · UniProt A0A7I9EWC2 · UniProt A0A6A5Q7Q6 · UniProt A0A6A5Q7A1 · UniProt A0A6A5PY05 · UniProt P41895 · UniProt A0A6A5PZ00
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.