MolNFT v1 · #51681 · protein
Structural model for the complex between the dr adhesins and carcinoembryonic antigen (cea)
2VER · Afimbrial adhesin afa-III: “Structural model for the complex between the dr adhesins and carcinoembryonic antigen (cea)”. Solution nmr, 1 ligand (MTN). MolNFT v1 #51681 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2VER
- Type
- protein
- Length
- 253 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Afimbrial adhesin afa-III; Arcinoembryonic antigen-related cell adhesion molecule 5
- UniProt
- Q57254, P06731
- Ligands
- MTN
Structure
solution nmr · 2 distinct chains · 2% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Afimbrial adhesin afa-III | protein | 143 | 0% helix, 49% strand | Q57254 |
| N | Arcinoembryonic antigen-related cell adhesion molecule 5 | protein | 110 | 5% helix, 50% strand | P06731 |
Ligands and binding sites
- MTN · S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate · ligand · 3 copies · chains A, N
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–N · 721 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 covalent, 1 disulfide (covalent ligand, disulfide).
Compared structures
- 2VER · Structural model for the complex between the Dr adhesins and carcinoembryonic antigen… · the same entry in another collection · chain A against A, TM-score 1.00
- P06731 · AlphaFold monomer V2.0 prediction for carcinoembryonic antigen- related cell adhesion… · a predicted model of the same protein · chain N against A, TM-score 0.96
- Q57254 · AlphaFold monomer V2.0 prediction for afimbrial adhesin afa-III (Q57254) · 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 Q57254
- Every structure of UniProt P06731
- Elsewhere: RCSB PDB 2VER · PDBe 2VER · UniProt Q57254 · UniProt P06731
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