Research workbench
Crystal structure of chorismate mutase from bartonella henselae str. houston-1 in complex with malate
Analyse Crystal structure of chorismate mutase from bartonella henselae str. houston-1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RMI
- Type
- protein
- Length
- 105 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chorismate mutase protein
- EC
- 5.4.99.5
- UniProt
- Q6G5B4
- Ligands
- MLT
- Pockets
- 1 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 88% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chorismate mutase protein (EC 5.4.99.5) | protein | 105 | 88% helix, 0% strand | Q6G5B4 |
Ligands and binding sites
- MLT · D-malate · ligand · chains A
- EDO · 1,2-ethanediol · additive · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 69 | 0.44 | 0.82 | 13 | empty |
Compared structures
- 3RMI · Crystal structure of Chorismate mutase from Bartonella henselae str. Houston-1 in complex… · 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 Q6G5B4
- Elsewhere: RCSB PDB 3RMI · PDBe 3RMI · UniProt Q6G5B4
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