Crystal structure of a clathrin heavy chain and clathrin light chain complex. Determined by X-ray diffraction at 9.0 Å resolution. Released 9 Jun 2010.
Explore 3LVH in 3D Show helices and sheets RCSB PDB PDBe
3LVH contains 127 α-helices and 8 β-strands across 6 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 | 1111-1114 | 4 | |
| α-helix | 1138-1143 | 6 | |
| α-helix | 1153-1164 | 12 | |
| α-helix | 1171-1178 | 8 | |
| α-helix | 1198-1207 | 10 | |
| α-helix | 1218-1220 | 3 | |
| β-strand | 1235 | 1 | 1 |
| β-strand | 1237 | 1 | 1 |
| α-helix | 1244-1246 | 3 | |
| α-helix | 1253-1256 | 4 | |
| α-helix | 1258-1262 | 5 | |
| α-helix | 1271-1277 | 7 | |
| α-helix | 1285-1287 | 3 | |
| α-helix | 1296-1298 | 3 | |
| α-helix | 1303-1306 | 4 | |
| α-helix | 1314-1325 | 12 | |
| α-helix | 1331-1336 | 6 | |
| α-helix | 1349-1352 | 4 | |
| α-helix | 1358-1368 | 11 | |
| α-helix | 1371-1376 | 6 | |
| α-helix | 1382-1385 | 4 | |
| α-helix | 1388-1391 | 4 | |
| α-helix | 1395-1397 | 3 | |
| α-helix | 1402-1408 | 7 | |
| α-helix | 1409-1413 | 5 | |
| α-helix | 1420-1426 | 7 | |
| α-helix | 1436-1440 | 5 | |
| α-helix | 1445-1448 | 4 | |
| α-helix | 1450-1452 | 3 | |
| α-helix | 1461-1473 | 13 | |
| α-helix | 1478-1482 | 5 | |
| α-helix | 1494-1500 | 7 | |
| α-helix | 1505-1516 | 12 | |
| α-helix | 1520-1524 | 5 | |
| α-helix | 1536-1538 | 3 | |
| α-helix | 1549-1560 | 12 | |
| α-helix | 1564-1573 | 10 | |
| α-helix | 1580-1588 | 9 | |
| α-helix | 1606-1628 | 23 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1111-1114 | 4 | |
| α-helix | 1138-1143 | 6 | |
| α-helix | 1153-1164 | 12 | |
| α-helix | 1171-1178 | 8 | |
| α-helix | 1198-1207 | 10 | |
| α-helix | 1218-1220 | 3 | |
| β-strand | 1235 | 1 | 2 |
| β-strand | 1237 | 1 | 2 |
| α-helix | 1244-1246 | 3 | |
| α-helix | 1253-1256 | 4 | |
| α-helix | 1258-1262 | 5 | |
| α-helix | 1271-1277 | 7 | |
| α-helix | 1285-1287 | 3 | |
| β-strand | 1293 | 1 | 3 |
| α-helix | 1296-1298 | 3 | |
| α-helix | 1303-1306 | 4 | |
| α-helix | 1314-1325 | 12 | |
| α-helix | 1331-1336 | 6 | |
| α-helix | 1349-1352 | 4 | |
| α-helix | 1358-1368 | 11 | |
| α-helix | 1371-1376 | 6 | |
| α-helix | 1382-1385 | 4 | |
| α-helix | 1388-1391 | 4 | |
| α-helix | 1395-1397 | 3 | |
| α-helix | 1402-1408 | 7 | |
| α-helix | 1409-1413 | 5 | |
| α-helix | 1420-1426 | 7 | |
| α-helix | 1436-1440 | 5 | |
| α-helix | 1445-1448 | 4 | |
| α-helix | 1450-1452 | 3 | |
| α-helix | 1461-1473 | 13 | |
| α-helix | 1478-1482 | 5 | |
| α-helix | 1494-1500 | 7 | |
| α-helix | 1505-1516 | 12 | |
| α-helix | 1520-1524 | 5 | |
| α-helix | 1536-1538 | 3 | |
| α-helix | 1549-1560 | 12 | |
| α-helix | 1564-1573 | 10 | |
| α-helix | 1580-1588 | 9 | |
| α-helix | 1606-1628 | 23 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 97 | 1 | 3 |
| α-helix | 101-109 | 9 | |
| α-helix | 115-151 | 37 | |
| α-helix | 162-168 | 7 | |
| α-helix | 176-182 | 7 | |
| α-helix | 195-204 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 101-109 | 9 | |
| α-helix | 115-151 | 37 | |
| α-helix | 171-178 | 8 | |
| α-helix | 188-191 | 4 | |
| α-helix | 193-200 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 103-109 | 7 | |
| α-helix | 115-151 | 37 | |
| α-helix | 171-180 | 10 | |
| α-helix | 183-186 | 4 | |
| α-helix | 188-190 | 3 | |
| α-helix | 192-200 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Clathrin heavy chain 1 | A, B, C | protein | 624 | Bos taurus | P49951 (AlphaFold model) |
| Clathrin light chain B | D, E, F | protein | 205 | Bos taurus | P04975 (AlphaFold model) |
>3LVH_1 Clathrin heavy chain 1 (chains A, B, C) MGSSHHHHHHSSGLVPRGSHMLKFDVNTSAVQVLIEHIGNLDRAYEFAERCNEPAVWSQL AKAQLQKGMVKEAIDSYIKADDPSSYMEVVQAANTSGNWEELVKYLQMARKKARESYVET ELIFALAKTNRLAELEEFINGPNNAHIQQVGDRCYDEKMYDAAKLLYNNVSNFGRLASTL VHLGEYQAAVDGARKANSTRTWKEVCFACVDGKEFRLAQMCGLHIVVHADELEELINYYQ DRGYFEELITMLEAALGLERAHMGMFTELAILYSKFKPQKMREHLELFWSRVNIPKVLRA AEQAHLWAELVFLYDKYEEYDNAIITMMNHPTDAWKEGQFKDIITKVANVELYYRAIQFY LEFKPLLLNDLLMVLSPRLDHTRAVNYFSKVKQLPLVKPYLRSVQNHNNKSVNESLNNLF ITEEDYQALRTSIDAYDNFDNISLAQRLEKHELIEFRRIAAYLFKGNNRWKQSVELCKKD SLYKDAMQYASESKDTELAEELLQWFLQEEKRECFGACLFTCYDLLRPDVVLETAWRHNI MDFAMPYFIQVMKEYLTKVDKLDASESLRKEEEQATETQPIVYGQPQLMLTAGPSVAVPP QAPFGYGYTAPAYGQPQPGFGYSM
>3LVH_2 Clathrin light chain B (chains D, E, F) MADDFGFFSSSESGAPEAAEEDPAAAFLAQQESEIAGIENDEGFGAPAGSQGGLAQPGPA SGASEDMGATVNGDVFQEANGPADGYAAIAQADRLTQEPESIRKWREEQRKRLQELDAAS KVMEQEWREKAKKDLEEWNQRQSEQVEKNKINNRIADKAFYQQPDADIIXXXXXXXXXXX XXXXXXXXXXXXXXXXXXXXXXXXX
Conformation switching of clathrin light chain regulates clathrin lattice assembly. Wilbur, J.D., Hwang, P.K., Ybe, J.A. et al. Dev Cell (2010) 18:841-848. DOI 10.1016/j.devcel.2010.04.007 · PubMed
Other PDB entries of the same protein (UniProt P49951 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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