Crystal structure of YgjG in complex with Pyridoxal-5'-phosphate and putrescine. Determined by X-ray diffraction at 2.08 Å resolution. Released 10 Dec 2014.
Explore 4UOX in 3D Show helices and sheets RCSB PDB PDBe
4UOX contains 100 α-helices and 76 β-strands across 4 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 |
|---|---|---|---|
| α-helix | 10-22 | 13 | |
| α-helix | 28-41 | 14 | |
| α-helix | 42-46 | 5 | |
| α-helix | 48-56 | 9 | |
| α-helix | 60-62 | 3 | |
| β-strand | 66 | 1 | 1 |
| β-strand | 67-70 | 4 | 2 |
| β-strand | 75-78 | 4 | 2 |
| β-strand | 83-86 | 4 | 2 |
| α-helix | 89-91 | 3 | |
| α-helix | 101-113 | 13 | |
| β-strand | 122 | 1 | 3 |
| α-helix | 124-136 | 13 | |
| β-strand | 141-147 | 7 | 4 |
| α-helix | 150-165 | 16 | |
| β-strand | 172-176 | 5 | 4 |
| α-helix | 185-190 | 6 | |
| α-helix | 194-197 | 4 | |
| α-helix | 198-200 | 3 | |
| β-strand | 207-210 | 4 | 4 |
| α-helix | 215-228 | 14 | |
| β-strand | 232-237 | 6 | 4 |
| β-strand | 241 | 1 | 5 |
| β-strand | 247 | 1 | 5 |
| α-helix | 248-250 | 3 | |
| α-helix | 253-264 | 12 | |
| α-helix | 266 | 1 | |
| β-strand | 267-271 | 5 | 4 |
| α-helix | 285-287 | 3 | |
| β-strand | 295-298 | 4 | 4 |
| α-helix | 300-303 | 4 | |
| β-strand | 310-315 | 6 | 4 |
| α-helix | 316-319 | 4 | |
| α-helix | 320-322 | 3 | |
| α-helix | 337-352 | 16 | |
| α-helix | 355-376 | 22 | |
| β-strand | 381-387 | 7 | 6 |
| β-strand | 390-395 | 6 | 6 |
| α-helix | 398-410 | 13 | |
| β-strand | 413-414 | 2 | 2 |
| β-strand | 416 | 1 | 6 |
| β-strand | 424-427 | 4 | 6 |
| α-helix | 435-456 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-22 | 13 | |
| α-helix | 28-41 | 14 | |
| α-helix | 42-46 | 5 | |
| α-helix | 48-56 | 9 | |
| α-helix | 62-64 | 3 | |
| β-strand | 66 | 1 | 3 |
| β-strand | 67-70 | 4 | 7 |
| β-strand | 75-78 | 4 | 7 |
| β-strand | 83-86 | 4 | 7 |
| α-helix | 89-91 | 3 | |
| α-helix | 101-113 | 13 | |
| β-strand | 122 | 1 | 1 |
| α-helix | 123 | 1 | |
| α-helix | 124-136 | 13 | |
| β-strand | 141-147 | 7 | 8 |
| α-helix | 150-165 | 16 | |
| α-helix | 166-168 | 3 | |
| β-strand | 172-176 | 5 | 8 |
| α-helix | 185-188 | 4 | |
| α-helix | 194-197 | 4 | |
| α-helix | 198-200 | 3 | |
| β-strand | 207-210 | 4 | 8 |
| α-helix | 215-228 | 14 | |
| β-strand | 232-237 | 6 | 8 |
| β-strand | 241 | 1 | 9 |
| β-strand | 247 | 1 | 9 |
| α-helix | 248-250 | 3 | |
| α-helix | 253-264 | 12 | |
| α-helix | 266 | 1 | |
| β-strand | 267-271 | 5 | 8 |
| α-helix | 285-288 | 4 | |
| β-strand | 295-298 | 4 | 8 |
| α-helix | 300-303 | 4 | |
| β-strand | 310-315 | 6 | 8 |
| α-helix | 316-319 | 4 | |
| α-helix | 320-322 | 3 | |
| α-helix | 337-352 | 16 | |
| α-helix | 355-376 | 22 | |
| β-strand | 381-387 | 7 | 10 |
| β-strand | 390-395 | 6 | 10 |
| α-helix | 398-410 | 13 | |
| β-strand | 413-414 | 2 | 7 |
| β-strand | 416-418 | 3 | 10 |
| β-strand | 421-427 | 7 | 10 |
| α-helix | 435-456 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-22 | 13 | |
| α-helix | 28-41 | 14 | |
| α-helix | 42-46 | 5 | |
| α-helix | 48-54 | 7 | |
| α-helix | 60-64 | 5 | |
| β-strand | 66 | 1 | 11 |
| β-strand | 67-70 | 4 | 12 |
| β-strand | 75-78 | 4 | 12 |
| β-strand | 83-86 | 4 | 12 |
| α-helix | 89-92 | 4 | |
| α-helix | 101-111 | 11 | |
| β-strand | 122 | 1 | 13 |
| α-helix | 124-136 | 13 | |
| β-strand | 141-147 | 7 | 14 |
| α-helix | 150-165 | 16 | |
| α-helix | 166-168 | 3 | |
| β-strand | 172-176 | 5 | 14 |
| α-helix | 185-190 | 6 | |
| α-helix | 194-197 | 4 | |
| α-helix | 198-200 | 3 | |
| β-strand | 207-210 | 4 | 14 |
| α-helix | 215-228 | 14 | |
| β-strand | 232-237 | 6 | 14 |
| β-strand | 241 | 1 | 15 |
| β-strand | 247 | 1 | 15 |
| α-helix | 248-250 | 3 | |
| α-helix | 253-264 | 12 | |
| α-helix | 266 | 1 | |
| β-strand | 267-271 | 5 | 14 |
| α-helix | 285-287 | 3 | |
| β-strand | 295-298 | 4 | 14 |
| α-helix | 300-303 | 4 | |
| β-strand | 310-315 | 6 | 14 |
| α-helix | 316-319 | 4 | |
| α-helix | 320-322 | 3 | |
| α-helix | 337-352 | 16 | |
| α-helix | 355-376 | 22 | |
| β-strand | 381-387 | 7 | 16 |
| β-strand | 390-395 | 6 | 16 |
| α-helix | 399-410 | 12 | |
| β-strand | 413-414 | 2 | 12 |
| β-strand | 416-418 | 3 | 16 |
| β-strand | 421-427 | 7 | 16 |
| α-helix | 435-456 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-22 | 13 | |
| α-helix | 28-41 | 14 | |
| α-helix | 42-46 | 5 | |
| α-helix | 48-56 | 9 | |
| α-helix | 60-64 | 5 | |
| β-strand | 66 | 1 | 13 |
| β-strand | 67-72 | 6 | 17 |
| β-strand | 75-78 | 4 | 17 |
| β-strand | 83-86 | 4 | 17 |
| α-helix | 89-92 | 4 | |
| α-helix | 101-113 | 13 | |
| β-strand | 122 | 1 | 11 |
| α-helix | 123 | 1 | |
| α-helix | 124-136 | 13 | |
| β-strand | 141-147 | 7 | 18 |
| α-helix | 150-165 | 16 | |
| α-helix | 166-168 | 3 | |
| β-strand | 172-176 | 5 | 18 |
| α-helix | 185-190 | 6 | |
| α-helix | 194-197 | 4 | |
| α-helix | 198-200 | 3 | |
| β-strand | 207-210 | 4 | 18 |
| α-helix | 215-227 | 13 | |
| β-strand | 232-237 | 6 | 18 |
| β-strand | 241 | 1 | 19 |
| β-strand | 247 | 1 | 19 |
| α-helix | 248-250 | 3 | |
| α-helix | 253-264 | 12 | |
| β-strand | 267-271 | 5 | 18 |
| α-helix | 285-287 | 3 | |
| β-strand | 295-298 | 4 | 18 |
| α-helix | 300-303 | 4 | |
| β-strand | 310-315 | 6 | 18 |
| α-helix | 316-319 | 4 | |
| α-helix | 320-322 | 3 | |
| α-helix | 337-352 | 16 | |
| α-helix | 355-376 | 22 | |
| β-strand | 381-387 | 7 | 20 |
| β-strand | 390-395 | 6 | 20 |
| α-helix | 398-410 | 13 | |
| β-strand | 413-414 | 2 | 17 |
| β-strand | 416-418 | 3 | 20 |
| β-strand | 421-427 | 7 | 20 |
| α-helix | 435-458 | 24 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Putrescine aminotransferase | A, B, C, D | protein | 467 | ESCHERICHIA COLI | P42588 (AlphaFold model) |
>4UOX_1 PUTRESCINE AMINOTRANSFERASE (chains A, B, C, D) MNRLPSSASALACSAHALNLIEKRTLDHEEMKALNREVIEYFKEHVNPGFLEYRKSVTAG GDYGAVEWQAGSLNTLVDTQGQEFIDCLGGFGIFNVGHRNPVVVSAVQNQLAKQPLHSQE LLDPLRAMLAKTLAALTPGKLKYSFFCNSGTESVEAALKLAKAYQSPRGKFTFIATSGAF HGKSLGALSATAKSTFRKPFMPLLPGFRHVPFGNIEAMRTALNECKKTGDDVAAVILEPI QGEGGVILPPPGYLTAVRKLCDEFGALMILDEVQTGMGRTGKMFACEHENVQPDILCLAK ALGGGVMPIGATIATEEVFSVLFDNPFLHTTTFGGNPLACAAALATINVLLEQNLPAQAE QKGDMLLDGFRQLAREYPDLVQEARGKGMLMAIEFVDNEIGYNFASEMFRQRVLVAGTLN NAKTIRIEPPLTLTIEQCELVIKAARKALAAMRVSVEEALEHHHHHH
Water and common crystallization additives (FMT, GOL, PEG) are not listed.
Structure of Putrescine Aminotransferase from Escherichia Coli Provides Insights Into the Substrate Specificity Among Class III Aminotransferases. Cha, H.J., Jeong, J., Rojviriya, C. et al. PLoS One (2014) 9:13212. DOI 10.1371/JOURNAL.PONE.0113212 · PubMed
Other PDB entries of the same protein (UniProt P42588 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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