Research workbench
Crystal structure of the hasap V37G/K59Q mutant capturing iron tetraphenylporphyrin
Analyse Crystal structure of the hasap V37G/K59Q mutant capturing iron… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EMW
- Type
- protein
- Length
- 172 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heme acquisition protein hasap
- UniProt
- G3XD33
- Ligands
- MQP
- Pockets
- 1 · best druggability 0.33
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heme acquisition protein hasap | protein | 172 | 31% helix, 39% strand | G3XD33 |
Ligands and binding sites
- MQP · [5,10,15,20-tetraphenylporphyrinato(2-)-kappa~4~n~21~, n~22~,n~23~,n~24~]iron · ligand · 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 | 58 | 0.33 | 0.76 | 10 | empty |
Compared structures
- 7EMW · Crystal Structure of the HasAp V37G/K59Q Mutant Capturing Iron Tetraphenylporphyrin · 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 G3XD33
- Elsewhere: RCSB PDB 7EMW · PDBe 7EMW · UniProt G3XD33
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