Research workbench
NMR solution structure of the two domain ppiase slpa from escherichia COLI
Analyse NMR solution structure of the two domain ppiase slpa from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2M2A
- Type
- protein
- Length
- 148 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fkbp-type 16 kda peptidyl-prolyl cis-trans isomerase
- EC
- 5.2.1.8
- UniProt
- P0AEM0
- Pockets
- 1 · best druggability 0.46
Structure
solution nmr · 1 distinct chain · 11% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fkbp-type 16 kda peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) | protein | 148 | 11% helix, 34% strand | P0AEM0 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 159 | 0.46 | 0.75 | 33 | empty |
Compared structures
- 2M2A · NMR solution structure of the two domain PPIase SlpA from Escherichia coli · the same entry in another collection · chain A against A, TM-score 1.00
- P0AEM0 · AlphaFold monomer V2.0 prediction for fkbp-type 16 kda peptidyl- prolyl cis-trans… · a predicted model of the same protein · chain A against A, TM-score 0.79
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 P0AEM0
- Elsewhere: RCSB PDB 2M2A · PDBe 2M2A · UniProt P0AEM0
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