Research workbench
Crystal structure of the extracellular portion of HAB18G/CD147
Analyse Crystal structure of the extracellular portion of HAB18G/CD147 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3B5H
- Type
- protein
- Length
- 721 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cervical emmprin
- UniProt
- Q54A51
- Pockets
- 6 · best druggability 0.71
Structure
x-ray diffraction · 3 distinct chains · 3% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cervical emmprin | protein | 181 | 3% helix, 55% strand | Q54A51 |
| C | Cervical emmprin | protein | 180 | 3% helix, 53% strand | Q54A51 |
| D | Cervical emmprin | protein | 179 | 2% helix, 54% strand | Q54A51 |
Ligands and binding sites
- ACT · Acetate ion · additive · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 678 | 0.71 | 0.78 | 64 | empty |
| 2 | 347 | 0.56 | 0.75 | 53 | empty |
| 3 | 114 | 0.39 | 0.75 | 27 | empty |
| 4 | 118 | 0.39 | 0.74 | 20 | empty |
| 5 | 71 | 0.38 | 0.78 | 18 | empty |
Interfaces
5 interfaces between chains.
- A–C · 553 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 450 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 425 Ų buried · 9 hydrogen bonds · protein-protein
- B–D · 204 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 74 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 3B5H · Crystal structure of the extracellular portion of HAb18G/CD147 · 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 Q54A51
- Elsewhere: RCSB PDB 3B5H · PDBe 3B5H · UniProt Q54A51
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