3LVG: Clathrin heavy chain 1
Crystal structure of a clathrin heavy chain and clathrin light chain complex. Determined by X-ray diffraction at 7.94 Å resolution. Released 9 Jun 2010.
- Method
- X-ray diffraction
- Resolution
- 7.94 Å
- Organism
- Bos taurus
- Chains
- 6
- Atoms
- 16,504
- Mol. weight
- 273.99 kDa
- Released
- 9 Jun 2010
Explore 3LVG in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3LVG contains 133 α-helices and 6 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.
Chain A: 37 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1087-1089 | 3 | |
| α-helix | 1111-1114 | 4 | |
| α-helix | 1135 | 1 | |
| α-helix | 1139-1143 | 5 | |
| α-helix | 1153-1158 | 6 | |
| α-helix | 1171-1178 | 8 | |
| α-helix | 1199-1207 | 9 | |
| α-helix | 1218-1220 | 3 | |
| β-strand | 1235 | 1 | 1 |
| β-strand | 1237 | 1 | 1 |
| α-helix | 1253-1256 | 4 | |
| α-helix | 1258-1262 | 5 | |
| α-helix | 1271-1277 | 7 | |
| α-helix | 1285-1287 | 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 | 1564-1572 | 9 | |
| α-helix | 1580-1588 | 9 | |
| α-helix | 1606-1628 | 23 | |
Chain B: 37 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1111-1114 | 4 | |
| α-helix | 1122-1125 | 4 | |
| α-helix | 1139-1143 | 5 | |
| α-helix | 1153-1158 | 6 | |
| α-helix | 1171-1178 | 8 | |
| α-helix | 1199-1207 | 9 | |
| α-helix | 1218-1220 | 3 | |
| β-strand | 1235 | 1 | 2 |
| β-strand | 1237 | 1 | 2 |
| 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 | |
| β-strand | 1428 | 1 | 3 |
| β-strand | 1430 | 1 | 3 |
| 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 | 1564-1572 | 9 | |
| α-helix | 1580-1585 | 6 | |
| α-helix | 1606-1624 | 19 | |
Chain C: 37 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1111-1114 | 4 | |
| α-helix | 1138-1143 | 6 | |
| α-helix | 1153-1160 | 8 | |
| α-helix | 1171-1178 | 8 | |
| α-helix | 1198-1206 | 9 | |
| α-helix | 1218-1220 | 3 | |
| α-helix | 1236-1238 | 3 | |
| 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 | 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 | 1564-1572 | 9 | |
| α-helix | 1580-1588 | 9 | |
| α-helix | 1606-1628 | 23 | |
Chain D: 9 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 39-42 | 4 | |
| α-helix | 49-51 | 3 | |
| α-helix | 52-57 | 6 | |
| α-helix | 61-71 | 11 | |
| 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 | |
Chain E: 6 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-6 | 3 | |
| 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 | |
Chain F: 7 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-7 | 5 | |
| 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 | |
Molecules and chains
| 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 | 190 | Bos taurus | P04975 (AlphaFold model) |
Sequence of entity 1 (A, B, C), FASTA
>3LVG_1 Clathrin heavy chain 1 (chains A, B, C)
MGSSHHHHHHSSGLVPRGSHMLKFDVNTSAVQVLIEHIGNLDRAYEFAERCNEPAVWSQL
AKAQLQKGMVKEAIDSYIKADDPSSYMEVVQAANTSGNWEELVKYLQMARKKARESYVET
ELIFALAKTNRLAELEEFINGPNNAHIQQVGDRCYDEKMYDAAKLLYNNVSNFGRLASTL
VHLGEYQAAVDGARKANSTRTWKEVCFACVDGKEFRLAQMCGLHIVVHADELEELINYYQ
DRGYFEELITMLEAALGLERAHMGMFTELAILYSKFKPQKMREHLELFWSRVNIPKVLRA
AEQAHLWAELVFLYDKYEEYDNAIITMMNHPTDAWKEGQFKDIITKVANVELYYRAIQFY
LEFKPLLLNDLLMVLSPRLDHTRAVNYFSKVKQLPLVKPYLRSVQNHNNKSVNESLNNLF
ITEEDYQALRTSIDAYDNFDNISLAQRLEKHELIEFRRIAAYLFKGNNRWKQSVELCKKD
SLYKDAMQYASESKDTELAEELLQWFLQEEKRECFGACLFTCYDLLRPDVVLETAWRHNI
MDFAMPYFIQVMKEYLTKVDKLDASESLRKEEEQATETQPIVYGQPQLMLTAGPSVAVPP
QAPFGYGYTAPAYGQPQPGFGYSM
Sequence of entity 2 (D, E, F), FASTA
>3LVG_2 Clathrin light chain B (chains D, E, F)
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXIAQADRLTQEPESIRKWREEQRKRLQELDAASKVMEQEWREKAKKDL
EEWNQRQSEQVEKNKINNRIADKAFYQQPDADIIXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXX
Primary citation
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:
- 5M5T 1.7 Å, Clathrin heavy chain N-terminal domain bound to a non-natural clathrin-box motif peptide…
- 9F8T 1.71 Å, Clathrin terminal domain complexed with C-terminus of AAK1L
- 5M5R 1.76 Å, Clathrin heavy chain N-terminal domain bound to beta2 adaptin clathrin box motif
- 5M61 1.84 Å, Clathrin heavy chain N-terminal domain bound to an extended amphiphysin clathrin-box motif
- 5M5S 1.88 Å, Clathrin heavy chain N-terminal domain bound to amphiphysin clathrin-box motif
- 5M5V 1.96 Å, Clathrin heavy chain N-terminal domain bound to a clathrin-box motif from hepatitis D…
- 5M5U 2.15 Å, Clathrin heavy chain N-terminal domain bound to a clathrin-box motif from hepatitis D…
- 3GC3 2.2 Å, Crystal Structure of Arrestin2S and Clathrin
- 1UTC 2.3 Å, Clathrin terminal domain complexed with TLPWDLWTT
- 1B89 2.6 Å, Clathrin heavy chain proximal leg segment (BOVINE)
- 3GD1 3.5 Å, Structure of an Arrestin/Clathrin complex reveals a novel clathrin binding domain that…
- 3QIL 3.92 Å, Crystal structure analysis of the clathrin trimerization domain
Browse structure collections
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