Research workbench
Crystal structure of the tail fiber GP53 from acinetobacter baumannii bacteriophage AP22
Analyse Crystal structure of the tail fiber GP53 from acinetobacter baumannii… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MTM
- Type
- protein
- Length
- 137 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative tail fiber protein
- UniProt
- I2GUG0
- Ligands
- NA, BR, SO3
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative tail fiber protein | protein | 137 | 9% helix, 40% strand | I2GUG0 |
Ligands and binding sites
- NA · Sodium ion · metal · 3 copies · chains A
- BR · Bromide ion · ion · 20 copies · chains A
- SO3 · Sulfite ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4MTM · Crystal structure of the tail fiber gp53 from Acinetobacter baumannii bacteriophage AP22 · 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 I2GUG0
- Elsewhere: RCSB PDB 4MTM · PDBe 4MTM · UniProt I2GUG0
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