Structural Characterisation of the Apo-form of Human Lactate Dehydrogenase M Isozyme. Determined by X-ray diffraction at 2.1 Å resolution. Released 30 Apr 2014.
Explore 4L4R in 3D Show helices and sheets RCSB PDB PDBe
4L4R contains 34 α-helices and 30 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 |
|---|---|---|---|
| α-helix | 3-7 | 5 | |
| β-strand | 21-25 | 5 | 1 |
| α-helix | 29-40 | 12 | |
| β-strand | 46-50 | 5 | 1 |
| α-helix | 54-65 | 12 | |
| α-helix | 68-70 | 3 | |
| β-strand | 75-79 | 5 | 1 |
| α-helix | 82-85 | 4 | |
| β-strand | 90-93 | 4 | 1 |
| α-helix | 97-100 | 4 | |
| α-helix | 105-126 | 22 | |
| α-helix | 130 | 1 | |
| β-strand | 131-134 | 4 | 1 |
| α-helix | 139-150 | 12 | |
| α-helix | 154-156 | 3 | |
| β-strand | 157-159 | 3 | 1 |
| α-helix | 163-177 | 15 | |
| α-helix | 181-183 | 3 | |
| β-strand | 184-185 | 2 | 2 |
| β-strand | 188-189 | 2 | 3 |
| β-strand | 190 | 1 | 1 |
| β-strand | 197-198 | 2 | 3 |
| α-helix | 200-202 | 3 | |
| β-strand | 204-205 | 2 | 2 |
| β-strand | 208-209 | 2 | 2 |
| α-helix | 210-213 | 4 | |
| α-helix | 227-244 | 18 | |
| α-helix | 249-263 | 15 | |
| β-strand | 268-275 | 8 | 1 |
| β-strand | 287-295 | 9 | 1 |
| β-strand | 298-302 | 5 | 1 |
| α-helix | 309-326 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-7 | 5 | |
| β-strand | 21-25 | 5 | 4 |
| α-helix | 29-40 | 12 | |
| β-strand | 46-50 | 5 | 4 |
| α-helix | 54-66 | 13 | |
| α-helix | 68-70 | 3 | |
| β-strand | 75-78 | 4 | 4 |
| α-helix | 82-85 | 4 | |
| β-strand | 90-93 | 4 | 4 |
| α-helix | 97-100 | 4 | |
| α-helix | 105-126 | 22 | |
| α-helix | 130 | 1 | |
| β-strand | 131-134 | 4 | 4 |
| α-helix | 139-150 | 12 | |
| α-helix | 154-156 | 3 | |
| β-strand | 157-159 | 3 | 4 |
| α-helix | 163-177 | 15 | |
| α-helix | 181-183 | 3 | |
| β-strand | 184-185 | 2 | 5 |
| β-strand | 188-189 | 2 | 6 |
| β-strand | 190 | 1 | 4 |
| β-strand | 197-198 | 2 | 6 |
| α-helix | 200-202 | 3 | |
| β-strand | 204-205 | 2 | 5 |
| β-strand | 208-209 | 2 | 5 |
| α-helix | 210-213 | 4 | |
| α-helix | 227-244 | 18 | |
| α-helix | 249-263 | 15 | |
| β-strand | 268-275 | 8 | 4 |
| β-strand | 287-295 | 9 | 4 |
| β-strand | 298-302 | 5 | 4 |
| α-helix | 309-326 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| L-lactate dehydrogenase A chain | A, H | protein | 339 | Homo sapiens | P00338 (AlphaFold model) |
>4L4R_1 L-lactate dehydrogenase A chain (chains A, H) ATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILMKDLADELALVDVIEDKLKGE MMDLQHGSLFLRTPKIVSGKDYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFII PNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERLGVH PLSCHGWVLGEHGDSSVPVWSGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEV IKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLYGIKDDVFLSVPCILGQNGIS DLVKVTLTSEEEARLKKSADTLWGIQKELQFLEHHHHHH
Structural characterization of the apo form and NADH binary complex of human lactate dehydrogenase. Dempster, S., Harper, S., Moses, J.E. et al. Acta Crystallogr D Biol Crystallogr (2014) 70:1484-1490. DOI 10.1107/S1399004714005422 · PubMed
Other PDB entries of the same protein (UniProt P00338 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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