Research workbench
Crystal structure of lid-truncated ADP-bound bip in an oligomeric state
Analyse Crystal structure of lid-truncated ADP-bound bip in an oligomeric state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7A4V
- Type
- protein
- Length
- 521 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoplasmic reticulum chaperone bip
- EC
- 3.6.4.10
- UniProt
- G3I8R9
- Ligands
- ADP, K
- Pockets
- 5 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endoplasmic reticulum chaperone bip (EC 3.6.4.10) | protein | 521 | 32% helix, 31% strand | G3I8R9 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- K · Potassium ion · metal · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 717 | 0.79 | 0.83 | 77 | ADP, K |
| 2 | 138 | 0.47 | 0.77 | 19 | empty |
| 3 | 85 | 0.42 | 0.78 | 19 | empty |
| 4 | 61 | 0.32 | 0.76 | 15 | empty |
| 5 | 60 | 0.32 | 0.76 | 16 | empty |
Compared structures
- 7A4V · Crystal structure of lid-truncated ADP-bound BiP in an oligomeric state · the same entry in another collection · chain A against A, TM-score 1.00
- G3I8R9 · AlphaFold monomer V2.0 prediction for endoplasmic reticulum chaperone bip (G3I8R9) · a predicted model of the same protein · chain A against A, TM-score 0.66
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 G3I8R9
- Elsewhere: RCSB PDB 7A4V · PDBe 7A4V · UniProt G3I8R9
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