Research workbench
Crystal structure of a putative thioesterase (PMT_2055) from prochlorococcus marinus str. mit 9313 at 1.50 a resolution
Analyse Crystal structure of a putative thioesterase (PMT_2055) from prochlorococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HX5
- Type
- protein
- Length
- 144 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein
- UniProt
- Q7V4A7
- Ligands
- ETX
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein | protein | 144 | 26% helix, 37% strand | Q7V4A7 |
Ligands and binding sites
- ETX · 2-ethoxyethanol · ligand · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 2HX5 · Crystal structure of a putative thioesterase (pmt_2055) from prochlorococcus marinus str.… · the same entry in another collection · chain A against A, TM-score 1.00
- Q7V4A7 · AlphaFold monomer V2.0 prediction for 1,4-dihydroxy-2-naphthoyl-CoA hydrolase (Q7V4A7) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q7V4A7
- Elsewhere: RCSB PDB 2HX5 · PDBe 2HX5 · UniProt Q7V4A7
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