Research workbench
Structure of the phage P2 baseplate in its activated conformation with sr
Analyse Structure of the phage P2 baseplate in its activated conformation with sr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2X53
- Type
- protein
- Length
- 7,638 residues
- Chains
- 27
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q1RNF7
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 1, Y, Z | — | protein | 372 | — | — |
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R | — | protein | 263 | — | Q1RNF7 |
| S, T, U, V, W, X | — | protein | 298 | — | — |
Compared structures
- 2X53 · Structure of the phage p2 baseplate in its activated conformation with Sr · the same entry in another collection · chain A against A, 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 Q1RNF7
- Elsewhere: RCSB PDB 2X53 · PDBe 2X53 · UniProt Q1RNF7
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