The Ligand-Free Structure of E coli BtuF, the Periplasmic Binding Protein for Vitamin B12. Determined by X-ray diffraction at 3.0 Å resolution. Released 11 Mar 2003.
Explore 1N4D in 3D Show helices and sheets RCSB PDB PDBe
1N4D contains 25 α-helices and 22 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 | 24-25 | 2 | 1 |
| α-helix | 33-37 | 5 | |
| β-strand | 40 | 1 | 1 |
| α-helix | 49-55 | 7 | |
| β-strand | 59-62 | 4 | 1 |
| α-helix | 64-66 | 3 | |
| α-helix | 69-77 | 9 | |
| β-strand | 82-84 | 3 | 1 |
| α-helix | 90-100 | 11 | |
| α-helix | 101-103 | 3 | |
| α-helix | 108-127 | 20 | |
| β-strand | 134-136 | 3 | 2 |
| β-strand | 137-138 | 2 | 3 |
| α-helix | 153-160 | 8 | |
| β-strand | 163-165 | 3 | 2 |
| α-helix | 166-169 | 4 | |
| α-helix | 179-184 | 6 | |
| β-strand | 190-192 | 3 | 3 |
| β-strand | 214-216 | 3 | 3 |
| α-helix | 217-218 | 2 | |
| α-helix | 219-222 | 4 | |
| α-helix | 229-241 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1004-1006 | 3 | 4 |
| α-helix | 1009-1017 | 9 | |
| β-strand | 1025 | 1 | 5 |
| α-helix | 1033-1037 | 5 | |
| β-strand | 1040 | 1 | 5 |
| β-strand | 1042 | 1 | 6 |
| β-strand | 1047 | 1 | 6 |
| α-helix | 1049-1055 | 7 | |
| β-strand | 1059-1062 | 4 | 4 |
| α-helix | 1069-1077 | 9 | |
| β-strand | 1082-1084 | 3 | 4 |
| α-helix | 1090-1099 | 10 | |
| α-helix | 1101-1103 | 3 | |
| α-helix | 1107-1124 | 18 | |
| β-strand | 1134-1136 | 3 | 7 |
| β-strand | 1137-1138 | 2 | 8 |
| α-helix | 1153-1160 | 8 | |
| β-strand | 1163-1165 | 3 | 7 |
| α-helix | 1181-1185 | 5 | |
| β-strand | 1190-1192 | 3 | 8 |
| β-strand | 1214-1216 | 3 | 8 |
| α-helix | 1219-1222 | 4 | |
| α-helix | 1229-1240 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vitamin B12 transport protein btuF | A, B | protein | 252 | Escherichia coli | P37028 (AlphaFold model) |
>1N4D_1 Vitamin B12 transport protein btuF (chains A, B) APRVITLSPANTELAFAAGITPVGVSSYSDYPPQAQKIEQVSTWQGMNLERIVALKPDLV IAWRGGNAERQVDQLASLGIKVMWVDATSIEQIANALRQLAPWSPQPDKAEQAAQSLLDQ YAQLKAQYADKPKKRVFLQFGINPPFTSGKESIQNQVLEVCGGENIFKDSRVPWPQVSRE QVLARSPQAIVITGGPDQIPKIKQYWGEQLKIPVIPLTSDWFERASPRIILAAQQLCNAL SQVDLEHHHHHH
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 1N4D 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.