5OVW: Vitamin B12-binding protein
Nanobody-bound BtuF, the vitamin B12 binding protein in Escherichia coli. Determined by X-ray diffraction at 2.65 Å resolution. Released 8 Nov 2017.
- Method
- X-ray diffraction
- Resolution
- 2.65 Å
- Organisms
- Escherichia coli, Lama glama
- Chains
- 12
- Atoms
- 17,352
- Mol. weight
- 291.32 kDa
- Released
- 8 Nov 2017
Explore 5OVW in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5OVW contains 129 α-helices and 150 β-strands across 12 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.
Chain A: 15 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 23-25 | 3 | |
| β-strand | 26-28 | 3 | 1 |
| α-helix | 31-39 | 9 | |
| β-strand | 46 | 1 | 1 |
| β-strand | 47-48 | 2 | 2 |
| α-helix | 55-59 | 5 | |
| α-helix | 61 | 1 | |
| β-strand | 62-65 | 4 | 2 |
| β-strand | 68-69 | 2 | 2 |
| α-helix | 71-76 | 6 | |
| β-strand | 81-84 | 4 | 1 |
| α-helix | 91-98 | 8 | |
| β-strand | 104-106 | 3 | 1 |
| α-helix | 112-122 | 11 | |
| α-helix | 123-125 | 3 | |
| α-helix | 129-149 | 21 | |
| β-strand | 156-161 | 6 | 3 |
| β-strand | 168 | 1 | 4 |
| α-helix | 175-182 | 8 | |
| β-strand | 185-187 | 3 | 3 |
| β-strand | 198 | 1 | 4 |
| α-helix | 201-206 | 6 | |
| β-strand | 211-214 | 4 | 3 |
| α-helix | 220-226 | 7 | |
| α-helix | 235 | 1 | |
| β-strand | 236-238 | 3 | 3 |
| α-helix | 241-244 | 4 | |
| α-helix | 251-262 | 12 | |
Chains B and E: 14 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 26-28 | 3 | 5 |
| α-helix | 31-39 | 9 | |
| β-strand | 46 | 1 | 5 |
| β-strand | 47-48 | 2 | 6 |
| α-helix | 55-59 | 5 | |
| α-helix | 61 | 1 | |
| β-strand | 62-65 | 4 | 6 |
| β-strand | 68-69 | 2 | 6 |
| α-helix | 71-76 | 6 | |
| β-strand | 81-84 | 4 | 5 |
| α-helix | 91-99 | 9 | |
| β-strand | 104-106 | 3 | 5 |
| α-helix | 112-122 | 11 | |
| α-helix | 123-125 | 3 | |
| α-helix | 129-149 | 21 | |
| β-strand | 156-161 | 6 | 7 |
| β-strand | 168 | 1 | 8 |
| α-helix | 175-182 | 8 | |
| β-strand | 185-187 | 3 | 7 |
| β-strand | 198 | 1 | 8 |
| α-helix | 201-206 | 6 | |
| β-strand | 211-214 | 4 | 7 |
| α-helix | 220-226 | 7 | |
| α-helix | 229-231 | 3 | |
| β-strand | 236-238 | 3 | 7 |
| α-helix | 241-244 | 4 | |
| α-helix | 251-262 | 12 | |
Chain C: 14 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 26-28 | 3 | 9 |
| α-helix | 31-39 | 9 | |
| β-strand | 46 | 1 | 9 |
| β-strand | 47-48 | 2 | 10 |
| α-helix | 55-58 | 4 | |
| α-helix | 61 | 1 | |
| β-strand | 62-65 | 4 | 10 |
| β-strand | 68-69 | 2 | 10 |
| α-helix | 71-76 | 6 | |
| β-strand | 81-84 | 4 | 9 |
| α-helix | 91-99 | 9 | |
| β-strand | 104-106 | 3 | 9 |
| α-helix | 112-122 | 11 | |
| α-helix | 123-125 | 3 | |
| α-helix | 129-149 | 21 | |
| β-strand | 156-161 | 6 | 11 |
| β-strand | 168 | 1 | 12 |
| α-helix | 175-182 | 8 | |
| β-strand | 185-187 | 3 | 11 |
| β-strand | 198 | 1 | 12 |
| α-helix | 201-206 | 6 | |
| β-strand | 211-214 | 4 | 11 |
| α-helix | 220-226 | 7 | |
| α-helix | 229-231 | 3 | |
| β-strand | 236-238 | 3 | 11 |
| α-helix | 241-244 | 4 | |
| α-helix | 251-262 | 12 | |
Chain D: 15 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 23-25 | 3 | |
| β-strand | 26-28 | 3 | 13 |
| α-helix | 31-39 | 9 | |
| β-strand | 46 | 1 | 13 |
| β-strand | 47-48 | 2 | 14 |
| α-helix | 55-59 | 5 | |
| α-helix | 61 | 1 | |
| β-strand | 62-65 | 4 | 14 |
| β-strand | 68-69 | 2 | 14 |
| α-helix | 71-76 | 6 | |
| β-strand | 81-84 | 4 | 13 |
| α-helix | 91-99 | 9 | |
| β-strand | 104-106 | 3 | 13 |
| α-helix | 112-122 | 11 | |
| α-helix | 123-125 | 3 | |
| α-helix | 129-149 | 21 | |
| β-strand | 156-161 | 6 | 15 |
| β-strand | 168 | 1 | 16 |
| α-helix | 175-182 | 8 | |
| β-strand | 185-187 | 3 | 15 |
| β-strand | 198 | 1 | 16 |
| α-helix | 201-206 | 6 | |
| β-strand | 211-214 | 4 | 15 |
| α-helix | 220-226 | 7 | |
| α-helix | 229-231 | 3 | |
| β-strand | 236-238 | 3 | 15 |
| α-helix | 241-244 | 4 | |
| α-helix | 251-262 | 12 | |
Chain F: 15 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 26-28 | 3 | 21 |
| α-helix | 31-39 | 9 | |
| β-strand | 46 | 1 | 21 |
| β-strand | 47-48 | 2 | 22 |
| α-helix | 55-59 | 5 | |
| α-helix | 61 | 1 | |
| β-strand | 62-65 | 4 | 22 |
| β-strand | 68-69 | 2 | 22 |
| α-helix | 71-76 | 6 | |
| β-strand | 81-84 | 4 | 21 |
| α-helix | 86-88 | 3 | |
| α-helix | 91-99 | 9 | |
| β-strand | 104-106 | 3 | 21 |
| α-helix | 112-122 | 11 | |
| α-helix | 123-125 | 3 | |
| α-helix | 129-149 | 21 | |
| β-strand | 156-161 | 6 | 23 |
| β-strand | 168 | 1 | 24 |
| α-helix | 175-182 | 8 | |
| β-strand | 185-187 | 3 | 23 |
| β-strand | 198 | 1 | 24 |
| α-helix | 201-206 | 6 | |
| β-strand | 211-214 | 4 | 23 |
| α-helix | 220-226 | 7 | |
| α-helix | 229-231 | 3 | |
| β-strand | 236-238 | 3 | 23 |
| α-helix | 241-244 | 4 | |
| α-helix | 251-262 | 12 | |
Chains G, I and J: 7 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 27-29 | 3 | 25 |
| α-helix | 34-35 | 2 | |
| β-strand | 40-45 | 6 | 25 |
| β-strand | 54-61 | 8 | 26 |
| α-helix | 66-67 | 2 | |
| β-strand | 68-73 | 6 | 26 |
| β-strand | 80-82 | 3 | 26 |
| β-strand | 90-95 | 6 | 25 |
| β-strand | 100-105 | 6 | 25 |
| α-helix | 110-112 | 3 | |
| β-strand | 114-122 | 9 | 26 |
| α-helix | 123-125 | 3 | |
| α-helix | 127-130 | 4 | |
| β-strand | 138-139 | 2 | 26 |
| α-helix | 140 | 1 | |
| β-strand | 141 | 1 | 25 |
| α-helix | 142 | 1 | |
| β-strand | 143-145 | 3 | 26 |
Chains H, K and L: 7 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 27-29 | 3 | 27 |
| β-strand | 34 | 1 | 28 |
| α-helix | 35 | 1 | |
| β-strand | 40-45 | 6 | 27 |
| β-strand | 54-61 | 8 | 29 |
| α-helix | 66-67 | 2 | |
| β-strand | 68-73 | 6 | 29 |
| β-strand | 80-82 | 3 | 29 |
| β-strand | 90-95 | 6 | 27 |
| β-strand | 100-105 | 6 | 27 |
| α-helix | 110-112 | 3 | |
| β-strand | 114-122 | 9 | 29 |
| α-helix | 123-125 | 3 | |
| α-helix | 127-130 | 4 | |
| β-strand | 138-139 | 2 | 29 |
| α-helix | 140 | 1 | |
| β-strand | 141 | 1 | 27 |
| α-helix | 142 | 1 | |
| β-strand | 143-145 | 3 | 29 |
| β-strand | 147 | 1 | 28 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Vitamin B12-binding protein | A, B, C, D, E, F | protein | 289 | Escherichia coli | P37028 (AlphaFold model) |
| Nanobody | G, H, I, J, K, L | protein | 159 | Lama glama | |
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>5OVW_1 Vitamin B12-binding protein (chains A, B, C, D, E, F)
MKKTAIAIAVALAGFATVAQAASMAAPRVITLSPANTELAFAAGITPVGVSSYSDYPPQA
QKIEQVSTWQGMNLERIVALKPDLVIAWRGGNAERQVDQLASLGIKVMWVDATSIEQIAN
ALRQLAPWSPQPDKAEQAAQSLLDQYAQLKAQYADKPKKRVFLQFGINPPFTSGKESIQN
QVLEVCGGENIFKDSRVPWPQVSREQVLARSPQAIVITGGPDQIPKIKQYWGEQLKIPVI
PLTSDWFERASPRIILAAQQLCNALSQVDSGSLEVLFQGPGGSHHHHHH
Sequence of entity 2 (G, H, I, J, K, L), FASTA
>5OVW_2 Nanobody (chains G, H, I, J, K, L)
MKYLLPTAAAGLLLLAAQPAMAQMQLVESGGGLVQPGGSLRLSCAAPESTLDDYAIGWFR
QAPGKEREGVSCIGSSGDSTNYADSVKGRFTVSRDNAKNTVYLQMNDLRPEDTAVYYCAA
AHRIFGGCLVIHSSGYVSWGQGTPVTVSSHHHHHHEPEA
Primary citation
Structural basis of nanobody-mediated blocking of BtuF, the cognate substrate-binding protein of the Escherichia coli vitamin B12 transporter BtuCD. Mireku, S.A., Sauer, M.M., Glockshuber, R. et al. Sci Rep (2017) 7:14296-14296. DOI 10.1038/s41598-017-14512-8 · PubMed
Other PDB entries of the same protein (UniProt P37028 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 5M29 1.5 Å, Structure of cobinamide-bound BtuF, the periplasmic vitamin B12 binding protein in E.coli
- 5M3B 1.5 Å, Structure of cobinamide-bound BtuF mutant W66L, the periplasmic vitamin B12 binding…
- 5M34 1.6 Å, Structure of cobinamide-bound BtuF mutant W66Y, the periplasmic vitamin B12 binding…
- 5M2Q 1.7 Å, Structure of cobinamide-bound BtuF mutant W66F, the periplasmic vitamin B12 binding…
- 1N2Z 2.0 Å, 2.0 Angstrom structure of BtuF, the vitamin B12 binding protein of E. coli
- 1N4A 2.0 Å, The Ligand Bound Structure of E.coli BtuF, the Periplasmic Binding Protein for Vitamin B12
- 2QI9 2.6 Å, ABC-transporter BtuCD in complex with its periplasmic binding protein BtuF
- 1N4D 3.0 Å, The Ligand-Free Structure of E coli BtuF, the Periplasmic Binding Protein for Vitamin B12
- 4FI3 3.47 Å, Structure of vitamin B12 transporter BtuCD-F in a nucleotide-bound state
- 4DBL 3.49 Å, Crystal structure of E159Q mutant of BtuCDF
Browse structure collections
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