4XGZ: Human paxillin LD2 motif
Crystal structure of human paxillin LD2 motif in complex with Fab fragment. Determined by X-ray diffraction at 2.5 Å resolution. Released 1 Jul 2015.
- Method
- X-ray diffraction
- Resolution
- 2.5 Å
- Organism
- Homo sapiens
- Chains
- 36
- Atoms
- 40,426
- Mol. weight
- 598.04 kDa
- Released
- 1 Jul 2015
Explore 4XGZ in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4XGZ contains 221 α-helices and 501 β-strands across 36 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.
Chains a, h, o, s, u and w: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-11 | 10 | |
Chain A: 11 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 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-39 | 7 | 2 |
| β-strand | 45-52 | 8 | 2 |
| β-strand | 56-59 | 4 | 2 |
| α-helix | 61-63 | 3 | |
| β-strand | 67-72 | 6 | 1 |
| β-strand | 77-82 | 6 | 1 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-96 | 9 | 2 |
| α-helix | 97-99 | 3 | |
| β-strand | 100-103 | 5 | 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 |
| 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 | 188-191 | 4 | |
| β-strand | 195-200 | 6 | 5 |
| α-helix | 201-203 | 3 | |
| β-strand | 205-210 | 6 | 5 |
| α-helix | 213-215 | 3 | |
Chains B, F, L, N, P, T and X: 8 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 9-13 | 5 | 6 |
| β-strand | 18-22 | 5 | 7 |
| α-helix | 23 | 1 | |
| 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 |
| 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 | 122-127 | 6 | |
| β-strand | 129-139 | 11 | 9 |
| β-strand | 140 | 1 | 8 |
| β-strand | 144-150 | 7 | 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 | 191-198 | 8 | 10 |
| β-strand | 205-210 | 6 | 10 |
Chain c: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-15 | 14 | |
Chain C: 10 helices, 22 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 11 |
| β-strand | 10-12 | 3 | 12 |
| β-strand | 18-25 | 8 | 11 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-39 | 7 | 12 |
| β-strand | 45-52 | 8 | 12 |
| β-strand | 56-59 | 4 | 12 |
| β-strand | 67-72 | 6 | 11 |
| β-strand | 77-82 | 6 | 11 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-96 | 9 | 12 |
| α-helix | 97-99 | 3 | |
| β-strand | 100-103 | 5 | 12 |
| β-strand | 107-111 | 5 | 12 |
| α-helix | 114-116 | 3 | |
| β-strand | 117 | 1 | 13 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 14 |
| α-helix | 125-127 | 3 | |
| β-strand | 135-145 | 11 | 14 |
| β-strand | 146 | 1 | 13 |
| β-strand | 151-154 | 4 | 15 |
| α-helix | 155-157 | 3 | |
| β-strand | 159 | 1 | 15 |
| β-strand | 163-165 | 3 | 14 |
| α-helix | 166-168 | 3 | |
| β-strand | 169-170 | 2 | 14 |
| β-strand | 176-185 | 10 | 14 |
| α-helix | 188-191 | 4 | |
| β-strand | 195-200 | 6 | 15 |
| α-helix | 201-203 | 3 | |
| β-strand | 205-210 | 6 | 15 |
Chains D, I and K: 7 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 9-13 | 5 | 16 |
| β-strand | 18-22 | 5 | 17 |
| β-strand | 32-38 | 7 | 16 |
| β-strand | 45-49 | 5 | 16 |
| β-strand | 53-54 | 2 | 16 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 17 |
| β-strand | 70-75 | 6 | 17 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-91 | 7 | 16 |
| β-strand | 96-98 | 3 | 16 |
| β-strand | 102-106 | 5 | 16 |
| β-strand | 111 | 1 | 18 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 19 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-127 | 6 | |
| β-strand | 129-139 | 11 | 19 |
| β-strand | 140 | 1 | 18 |
| β-strand | 144-150 | 7 | 20 |
| β-strand | 153-156 | 4 | 20 |
| β-strand | 159-163 | 5 | 19 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 19 |
| α-helix | 183-187 | 5 | |
| β-strand | 191-198 | 8 | 20 |
| β-strand | 205-210 | 6 | 20 |
Chains e, g and m: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-12 | 11 | |
Chain E: 10 helices, 22 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 21 |
| β-strand | 10-12 | 3 | 22 |
| β-strand | 17-25 | 9 | 21 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-39 | 7 | 22 |
| β-strand | 45-52 | 8 | 22 |
| β-strand | 56-59 | 4 | 22 |
| β-strand | 67-72 | 6 | 21 |
| β-strand | 77-82 | 6 | 21 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-96 | 9 | 22 |
| α-helix | 97-99 | 3 | |
| β-strand | 100-103 | 5 | 22 |
| α-helix | 104-106 | 3 | |
| 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 | 163-165 | 3 | 24 |
| α-helix | 166-168 | 3 | |
| β-strand | 169-170 | 2 | 24 |
| β-strand | 176-185 | 10 | 24 |
| α-helix | 186-188 | 3 | |
| β-strand | 195-200 | 6 | 25 |
| α-helix | 201-203 | 3 | |
| β-strand | 205-210 | 6 | 25 |
11 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, M, O, Q, S, U, W | protein | 229 | Homo sapiens | |
| FAB light chain | B, D, F, I, K, L, N, P, R, T, V, X | protein | 215 | Homo sapiens | |
| Paxillin LD2 | a, c, e, g, h, j, m, o, q, s, u, w | protein | 19 | Homo sapiens | P49023 (AlphaFold model) |
Sequence of entity 1 (A, C, E, G, H, J, M, O, Q, S, U, W), FASTA
>4XGZ_1 FAB HEAVY CHAIN (chains A, C, E, G, H, J, M, O, Q, S, U, W)
EISEVQLVESGGGLVQPGGSLRLSCAASGFNVSYSSIHWVRQAPGKGLEWVASIYSYYGY
TYYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARGYYGAAMDYWGQGTLVTVS
SASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQS
SGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT
Sequence of entity 2 (B, D, F, I, K, L, N, P, R, T, V, X), FASTA
>4XGZ_2 FAB LIGHT CHAIN (chains B, D, F, I, K, L, N, P, R, T, V, X)
SDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVP
SRFSGSRSGTDFTLTISSLQPEDFATYYCQQSSSSLITFGQGTKVEIKRTVAAPSVFIFP
PSDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL
TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
Sequence of entity 3 (a, c, e, g, h, j, m, o, q, s, u, w), FASTA
>4XGZ_3 PAXILLIN LD2 (chains a, c, e, g, h, j, m, o, q, s, u, w)
NLSELDRLLLELNAVQHNP
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…
- 4XH2 2.0 Å, Crystal structure of human paxillin LD4 motif in complex with Fab fragment
- 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
- 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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