The Ligand Bound Structure of E.coli BtuF, the Periplasmic Binding Protein for Vitamin B12. Determined by X-ray diffraction at 2.0 Å resolution. Released 11 Mar 2003.
Explore 1N4A in 3D Show helices and sheets RCSB PDB PDBe
1N4A contains 31 α-helices and 34 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-6 | 3 | 1 |
| α-helix | 9-17 | 9 | |
| β-strand | 24 | 1 | 1 |
| β-strand | 25-26 | 2 | 2 |
| α-helix | 33-37 | 5 | |
| α-helix | 39 | 1 | |
| β-strand | 40-42 | 3 | 2 |
| β-strand | 47 | 1 | 2 |
| α-helix | 49-54 | 6 | |
| β-strand | 59-63 | 5 | 1 |
| β-strand | 64 | 1 | 3 |
| β-strand | 67 | 1 | 3 |
| α-helix | 69-72 | 4 | |
| α-helix | 74-77 | 4 | |
| β-strand | 82-85 | 4 | 1 |
| α-helix | 90-100 | 11 | |
| α-helix | 101-103 | 3 | |
| α-helix | 107-128 | 22 | |
| α-helix | 132-133 | 2 | |
| β-strand | 134-138 | 5 | 4 |
| β-strand | 140 | 1 | 5 |
| β-strand | 146 | 1 | 5 |
| α-helix | 153-160 | 8 | |
| β-strand | 163-165 | 3 | 4 |
| β-strand | 176 | 1 | 5 |
| α-helix | 179-184 | 6 | |
| β-strand | 189-192 | 4 | 4 |
| α-helix | 196-198 | 3 | |
| α-helix | 199-206 | 8 | |
| α-helix | 207-209 | 3 | |
| β-strand | 214-216 | 3 | 4 |
| α-helix | 219-222 | 4 | |
| α-helix | 229-240 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5004-5006 | 3 | 6 |
| α-helix | 5009-5017 | 9 | |
| β-strand | 5024 | 1 | 6 |
| β-strand | 5025-5026 | 2 | 7 |
| α-helix | 5033-5037 | 5 | |
| α-helix | 5039 | 1 | |
| β-strand | 5040-5043 | 4 | 7 |
| β-strand | 5046-5047 | 2 | 7 |
| α-helix | 5049-5054 | 6 | |
| β-strand | 5059-5063 | 5 | 6 |
| β-strand | 5064 | 1 | 8 |
| β-strand | 5067 | 1 | 8 |
| α-helix | 5069-5077 | 9 | |
| β-strand | 5082-5085 | 4 | 6 |
| α-helix | 5090-5100 | 11 | |
| α-helix | 5101-5103 | 3 | |
| α-helix | 5107-5128 | 22 | |
| β-strand | 5134-5138 | 5 | 9 |
| β-strand | 5140 | 1 | 10 |
| β-strand | 5146 | 1 | 10 |
| α-helix | 5153-5160 | 8 | |
| β-strand | 5163-5165 | 3 | 9 |
| β-strand | 5176 | 1 | 10 |
| α-helix | 5179-5184 | 6 | |
| β-strand | 5189-5192 | 4 | 9 |
| β-strand | 5194 | 1 | 11 |
| α-helix | 5196-5198 | 3 | |
| α-helix | 5199-5206 | 8 | |
| β-strand | 5214-5216 | 3 | 9 |
| β-strand | 5218 | 1 | 11 |
| α-helix | 5219-5222 | 4 | |
| α-helix | 5229-5240 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vitamin B12 transport protein btuF | A, B | protein | 252 | Escherichia coli | P37028 (AlphaFold model) |
>1N4A_1 Vitamin B12 transport protein btuF (chains A, B) APRVITLSPANTELAFAAGITPVGVSSYSDYPPQAQKIEQVSTWQGMNLERIVALKPDLV IAWRGGNAERQVDQLASLGIKVMWVDATSIEQIANALRQLAPWSPQPDKAEQAAQSLLDQ YAQLKAQYADKPKKRVFLQFGINPPFTSGKESIQNQVLEVCGGENIFKDSRVPWPQVSRE QVLARSPQAIVITGGPDQIPKIKQYWGEQLKIPVIPLTSDWFERASPRIILAAQQLCNAL SQVDLEHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| CNC | Cyanocobalamin | C63 H89 Co N14 O14 P | 2 |
Crystal structures of the BtuF periplasmic-binding protein for vitamin B12 suggest a functionally important reduction in protein mobility upon ligand binding. Karpowich, N.K., Huang, H.H., Smith, P.C. et al. J Biol Chem (2003) 278:8429-8434. DOI 10.1074/jbc.M212239200 · PubMed
Other PDB entries of the same protein (UniProt P37028 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1N4A directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.