Research workbench
Crystal structure of the C-terminal nil domain of an ABC transporter protein homologue from staphylococcus aureus
Analyse Crystal structure of the C-terminal nil domain of an ABC transporter protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CED
- Type
- protein
- Length
- 294 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methionine import ATP-binding protein metn 2
- EC
- 3.6.3.-
- UniProt
- Q99VG8
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Methionine import ATP-binding protein metn 2 (EC 3.6.3.-) | protein | 98 | 37% helix, 38% strand | Q99VG8 |
Ligands and binding sites
- BU1 · 1,4-butanediol · additive · 4 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–C · 63 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 52 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 27 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 3CED · Crystal structure of the C-terminal NIL domain of an ABC transporter protein homologue… · the same entry in another collection · chain A against A, TM-score 1.00
- Q99VG8 · AlphaFold monomer V2.0 prediction for methionine import ATP-binding protein metn 2… · a predicted model of the same protein · chain A against A, TM-score 0.88
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 Q99VG8
- Elsewhere: RCSB PDB 3CED · PDBe 3CED · UniProt Q99VG8
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