4XH2: Human paxillin LD4 motif
Crystal structure of human paxillin LD4 motif in complex with Fab fragment. Determined by X-ray diffraction at 2.0 Å resolution. Released 1 Jul 2015.
- Method
- X-ray diffraction
- Resolution
- 2.0 Å
- Organisms
- Homo sapiens, synthetic construct
- Chains
- 18
- Atoms
- 21,729
- Mol. weight
- 301.9 kDa
- Ligands
- PO4, LDA, ACE
- Released
- 1 Jul 2015
Explore 4XH2 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4XH2 contains 106 α-helices and 256 β-strands across 18 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: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-14 | 11 | |
Chain A: 8 helices, 22 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 1 |
| β-strand | 10-12 | 3 | 2 |
| β-strand | 18-25 | 8 | 1 |
| β-strand | 34-39 | 6 | 2 |
| β-strand | 45-51 | 7 | 2 |
| β-strand | 57-59 | 3 | 2 |
| β-strand | 67-72 | 6 | 1 |
| β-strand | 77-82 | 6 | 1 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-95 | 8 | 2 |
| β-strand | 100A-103 | 4 | 2 |
| β-strand | 107-111 | 5 | 2 |
| α-helix | 114-116 | 3 | |
| β-strand | 117 | 1 | 3 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 4 |
| α-helix | 125-127 | 3 | |
| β-strand | 135-145 | 11 | 4 |
| β-strand | 146 | 1 | 3 |
| β-strand | 151-154 | 4 | 5 |
| α-helix | 155-157 | 3 | |
| β-strand | 159 | 1 | 5 |
| β-strand | 163-165 | 3 | 4 |
| α-helix | 166-168 | 3 | |
| β-strand | 169-170 | 2 | 4 |
| β-strand | 176-185 | 10 | 4 |
| α-helix | 186-190 | 5 | |
| β-strand | 195-200 | 6 | 5 |
| α-helix | 201-203 | 3 | |
| β-strand | 205-210 | 6 | 5 |
Chain B: 9 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-8 | 2 | |
| β-strand | 9-13 | 5 | 6 |
| β-strand | 18-22 | 5 | 7 |
| β-strand | 32-38 | 7 | 6 |
| β-strand | 45-49 | 5 | 6 |
| β-strand | 53-54 | 2 | 6 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 7 |
| β-strand | 70-75 | 6 | 7 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-91 | 7 | 6 |
| β-strand | 96-98 | 3 | 6 |
| α-helix | 99-101 | 3 | |
| β-strand | 102-106 | 5 | 6 |
| β-strand | 111 | 1 | 8 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 9 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| β-strand | 129-139 | 11 | 9 |
| β-strand | 140 | 1 | 8 |
| β-strand | 145-150 | 6 | 10 |
| β-strand | 153-156 | 4 | 10 |
| β-strand | 159-163 | 5 | 9 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 9 |
| α-helix | 183-187 | 5 | |
| β-strand | 191-197 | 7 | 10 |
| β-strand | 205-210 | 6 | 10 |
Chains c and h: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-14 | 8 | |
Chain C: 9 helices, 25 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 11 |
| β-strand | 11-12 | 2 | 12 |
| β-strand | 18-25 | 8 | 11 |
| β-strand | 34-39 | 6 | 13 |
| β-strand | 45-52 | 8 | 13 |
| β-strand | 56-59 | 4 | 13 |
| β-strand | 67-72 | 6 | 11 |
| β-strand | 77-82 | 6 | 11 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-95 | 8 | 13 |
| β-strand | 100A-103 | 4 | 13 |
| β-strand | 107-109 | 3 | 13 |
| β-strand | 110-111 | 2 | 12 |
| α-helix | 114-116 | 3 | |
| β-strand | 117 | 1 | 14 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 15 |
| α-helix | 125-126 | 2 | |
| β-strand | 127 | 1 | 16 |
| α-helix | 129-131 | 3 | |
| β-strand | 135-145 | 11 | 15 |
| β-strand | 146 | 1 | 14 |
| β-strand | 151-154 | 4 | 17 |
| α-helix | 155-157 | 3 | |
| β-strand | 159 | 1 | 17 |
| β-strand | 163-165 | 3 | 15 |
| α-helix | 166-168 | 3 | |
| β-strand | 169-170 | 2 | 15 |
| β-strand | 176-185 | 10 | 15 |
| α-helix | 186-188 | 3 | |
| β-strand | 195-200 | 6 | 17 |
| α-helix | 201-203 | 3 | |
| β-strand | 205-210 | 6 | 17 |
| β-strand | 214 | 1 | 16 |
Chain D: 8 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-8 | 2 | |
| β-strand | 9-13 | 5 | 18 |
| β-strand | 18-22 | 5 | 10 |
| β-strand | 32-38 | 7 | 18 |
| β-strand | 45-49 | 5 | 18 |
| β-strand | 53-54 | 2 | 18 |
| β-strand | 62-67 | 6 | 10 |
| β-strand | 70-75 | 6 | 10 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-91 | 7 | 18 |
| β-strand | 96-98 | 3 | 18 |
| α-helix | 99-101 | 3 | |
| β-strand | 102-106 | 5 | 18 |
| β-strand | 111 | 1 | 19 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 20 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| β-strand | 129-139 | 11 | 20 |
| β-strand | 140 | 1 | 19 |
| β-strand | 144-150 | 7 | 7 |
| β-strand | 153-156 | 4 | 7 |
| β-strand | 159-163 | 5 | 20 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 20 |
| α-helix | 183-186 | 4 | |
| β-strand | 191-198 | 8 | 7 |
| β-strand | 205-210 | 6 | 7 |
Chain e: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-15 | 13 | |
Chain E: 8 helices, 23 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 21 |
| β-strand | 10-12 | 3 | 22 |
| β-strand | 18-25 | 8 | 21 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 22 |
| β-strand | 45-51 | 7 | 22 |
| β-strand | 57-59 | 3 | 22 |
| β-strand | 67-72 | 6 | 21 |
| β-strand | 77-82 | 6 | 21 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-95 | 8 | 22 |
| β-strand | 100A-103 | 4 | 22 |
| β-strand | 107-111 | 5 | 22 |
| α-helix | 114-116 | 3 | |
| β-strand | 117 | 1 | 23 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 24 |
| β-strand | 135-145 | 11 | 24 |
| β-strand | 146 | 1 | 23 |
| β-strand | 151-154 | 4 | 25 |
| α-helix | 155-157 | 3 | |
| β-strand | 159 | 1 | 25 |
| β-strand | 164-165 | 2 | 24 |
| α-helix | 166-168 | 3 | |
| β-strand | 169-170 | 2 | 24 |
| β-strand | 176-185 | 10 | 24 |
| α-helix | 188-191 | 4 | |
| β-strand | 192 | 1 | 26 |
| β-strand | 195-200 | 6 | 25 |
| α-helix | 201-203 | 3 | |
| β-strand | 205-210 | 6 | 25 |
9 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Fab Heavy Chain | A, C, E, G, H, J | protein | 228 | Homo sapiens | |
| Fab Light Chain | B, D, F, I, K, L | protein | 217 | Homo sapiens | |
| paxillin LD4 | a, c, e, g, h, j | protein | 18 | synthetic construct | P49023 (AlphaFold model) |
Sequence of entity 1 (A, C, E, G, H, J), FASTA
>4XH2_1 Fab Heavy Chain (chains A, C, E, G, H, J)
EISEVQLVESGGGLVQPGGSLRLSCAASGFNVSSYSIHWVRQAPGKGLEWVAYISSSSGY
TYYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARTWYYGFDYWGQGTLVTVSS
ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSS
GLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT
Sequence of entity 2 (B, D, F, I, K, L), FASTA
>4XH2_2 Fab Light Chain (chains B, D, F, I, K, L)
SDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVP
SRFSGSRSGTDFTLTISSLQPEDFATYYCQQFKRQKEPITFGQGTKVEIKRTVAAPSVFI
FPPSDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSS
TLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
Sequence of entity 3 (a, c, e, g, h, j), FASTA
>4XH2_3 paxillin LD4 (chains a, c, e, g, h, j)
WGGSATRELDELMASLSD
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| PO4 | Phosphate ion | O4 P | 2 |
| LDA | Lauryl dimethylamine-N-oxide | C14 H31 N O | 1 |
| ACE | Acetyl group | C2 H4 O | 2 |
Water and common crystallization additives (GOL, ACT) are not listed.
Primary citation
Engineering Synthetic Antibody Inhibitors Specific for LD2 or LD4 Motifs of Paxillin. Nocula-Lugowska, M., Lugowski, M., Salgia, R. et al. J Mol Biol (2015) 427:2532-2547. DOI 10.1016/j.jmb.2015.06.004 · PubMed
Other PDB entries of the same protein (UniProt P49023 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 2O9V 1.63 Å, The second SH3 domain from Ponsin in complex with the paxillin proline rich region
- 2VZG 1.8 Å, Crystal structure of the C-terminal calponin homology domain of alpha- parvin in complex…
- 6PW8 1.95 Å, Hydrocarbon-Stapled Paxillin Peptide Bound to the Focal Adhesion Targeting (FAT) Domain…
- 2VZD 2.1 Å, Crystal structure of the C-terminal calponin homology domain of alpha parvin in complex…
- 2VZI 2.2 Å, Crystal structure of the C-terminal calponin homology domain of alpha- parvin in complex…
- 5UWH 2.26 Å, Crystal Structure of Paxillin NES Peptide in complex with CRM1-Ran-RanBP1
- 1OW6 2.35 Å, Paxillin LD4 motif bound to the Focal Adhesion Targeting (FAT) domain of the Focal…
- 3RQG 2.5 Å, Cerebral cavernous malformation 3 (CCM3) in complex with paxillin LD4
- 4XGZ 2.5 Å, Crystal structure of human paxillin LD2 motif in complex with Fab fragment
- 9QWO 2.54 Å, Vinculin tail bound to paxillin LD2
- 1OW7 2.6 Å, Paxillin LD4 motif bound to the Focal Adhesion Targeting (FAT) domain of the Focal…
- 6IUI 2.6 Å, Crystal structure of GIT1 PBD domain in complex with Paxillin LD4 motif
Browse structure collections
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