Neuropilin-2 a1a2b1b2 Domains in Complex with a Semaphorin-Blocking Fab. Determined by X-ray diffraction at 2.75 Å resolution. Released 20 Nov 2007.
Explore 2QQK in 3D Show helices and sheets RCSB PDB PDBe
2QQK contains 27 α-helices and 101 β-strands across 3 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 |
|---|---|---|---|
| β-strand | 30-33 | 4 | 1 |
| β-strand | 38-41 | 4 | 2 |
| α-helix | 48-50 | 3 | |
| β-strand | 55-60 | 6 | 1 |
| β-strand | 67-72 | 6 | 2 |
| β-strand | 77 | 1 | 3 |
| β-strand | 87-92 | 6 | 1 |
| β-strand | 99-104 | 6 | 1 |
| α-helix | 109-111 | 3 | |
| β-strand | 113-114 | 2 | 2 |
| β-strand | 119-125 | 7 | 1 |
| β-strand | 134 | 1 | 3 |
| β-strand | 136-142 | 7 | 2 |
| β-strand | 152-153 | 2 | 4 |
| β-strand | 157-161 | 5 | 5 |
| α-helix | 168-170 | 3 | |
| β-strand | 174-180 | 7 | 4 |
| β-strand | 185-195 | 11 | 5 |
| β-strand | 212-216 | 5 | 4 |
| α-helix | 224 | 1 | |
| β-strand | 225-229 | 5 | 4 |
| α-helix | 234-237 | 4 | |
| β-strand | 238-240 | 3 | 5 |
| β-strand | 244-250 | 7 | 4 |
| β-strand | 259-268 | 10 | 5 |
| β-strand | 279-280 | 2 | 6 |
| α-helix | 290-292 | 3 | |
| β-strand | 293-295 | 3 | 6 |
| α-helix | 306-308 | 3 | |
| β-strand | 310 | 1 | 6 |
| β-strand | 318 | 1 | 7 |
| β-strand | 329-345 | 17 | 6 |
| β-strand | 347-348 | 2 | 8 |
| β-strand | 355-356 | 2 | 8 |
| β-strand | 357-366 | 10 | 6 |
| β-strand | 373-374 | 2 | 6 |
| β-strand | 376-377 | 2 | 9 |
| β-strand | 380-381 | 2 | 9 |
| α-helix | 382-383 | 2 | |
| β-strand | 384-385 | 2 | 6 |
| β-strand | 394-415 | 22 | 6 |
| β-strand | 417 | 1 | 6 |
| β-strand | 420 | 1 | 7 |
| β-strand | 421-427 | 7 | 6 |
| α-helix | 429-431 | 3 | |
| β-strand | 436-437 | 2 | 10 |
| α-helix | 447-449 | 3 | |
| β-strand | 450-452 | 3 | 10 |
| α-helix | 462-465 | 4 | |
| β-strand | 466 | 1 | 10 |
| β-strand | 474 | 1 | 11 |
| β-strand | 488-504 | 17 | 10 |
| β-strand | 506 | 1 | 12 |
| β-strand | 519 | 1 | 12 |
| β-strand | 521-529 | 9 | 10 |
| β-strand | 536-537 | 2 | 10 |
| α-helix | 538 | 1 | |
| β-strand | 539 | 1 | 13 |
| α-helix | 540 | 1 | |
| β-strand | 546 | 1 | 13 |
| α-helix | 547 | 1 | |
| β-strand | 549-550 | 2 | 10 |
| β-strand | 559-578 | 20 | 10 |
| β-strand | 579 | 1 | 14 |
| β-strand | 582 | 1 | 14 |
| β-strand | 585 | 1 | 11 |
| β-strand | 586-592 | 7 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 15 |
| β-strand | 11-12 | 2 | 16 |
| β-strand | 18-25 | 8 | 15 |
| β-strand | 33-39 | 7 | 17 |
| β-strand | 45-52 | 8 | 17 |
| β-strand | 56-59 | 4 | 17 |
| β-strand | 67-72 | 6 | 15 |
| β-strand | 77-82 | 6 | 15 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-95 | 8 | 17 |
| α-helix | 100A-100C | 3 | |
| β-strand | 100G-103 | 4 | 17 |
| β-strand | 107-109 | 3 | 17 |
| β-strand | 110-111 | 2 | 16 |
| β-strand | 117 | 1 | 18 |
| β-strand | 120-124 | 5 | 19 |
| β-strand | 136-145 | 10 | 19 |
| β-strand | 146 | 1 | 18 |
| β-strand | 151-154 | 4 | 20 |
| α-helix | 155-157 | 3 | |
| β-strand | 159 | 1 | 20 |
| β-strand | 163-165 | 3 | 19 |
| α-helix | 166-168 | 3 | |
| β-strand | 169-170 | 2 | 19 |
| β-strand | 176-184 | 9 | 19 |
| α-helix | 186-188 | 3 | |
| β-strand | 189 | 1 | 21 |
| β-strand | 192 | 1 | 21 |
| β-strand | 195-199 | 5 | 20 |
| β-strand | 200 | 1 | 22 |
| α-helix | 201-203 | 3 | |
| β-strand | 205 | 1 | 22 |
| β-strand | 208-210 | 3 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 23 |
| β-strand | 10-14 | 5 | 24 |
| β-strand | 19-25 | 7 | 23 |
| β-strand | 33-38 | 6 | 24 |
| β-strand | 45-49 | 5 | 24 |
| β-strand | 53-54 | 2 | 24 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 23 |
| β-strand | 70-75 | 6 | 23 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-90 | 7 | 24 |
| β-strand | 97-98 | 2 | 24 |
| β-strand | 102-107 | 6 | 24 |
| β-strand | 111 | 1 | 25 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 26 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-125 | 4 | |
| β-strand | 130-139 | 10 | 26 |
| β-strand | 140 | 1 | 25 |
| β-strand | 145-150 | 6 | 27 |
| β-strand | 153-154 | 2 | 27 |
| β-strand | 159-163 | 5 | 26 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-181 | 9 | 26 |
| α-helix | 183-188 | 6 | |
| β-strand | 192-197 | 6 | 27 |
| β-strand | 205-209 | 5 | 27 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Neuropilin-2 | A | protein | 579 | Homo sapiens | O60462 (AlphaFold model) |
| Antibody Heavy Chain | H | protein | 231 | Homo sapiens | P01857 (AlphaFold model) |
| Antibody Light Chain | L | protein | 214 | Homo sapiens | P01834 (AlphaFold model) |
>2QQK_1 Neuropilin-2 (chains A) QPDPPCGGRLNSKDAGYITSPGYPQDYPSHQNCEWIVYAPEPNQKIVLNFNPHFEIEKHD CKYDFIEIRDGDSESADLLGKHCGNIAPPTIISSGSMLYIKFTSDYARQGAGFSLRYEIF KTGSEDCSKNFTSPNGTIESPGFPEKYPHNLDCTFTILAKPKMEIILQFLIFDLEHDPLQ VGEGDCKYDWLDIWDGIPHVGPLIGKYCGTKTPSELRSSTGILSLTFHTDMAVAKDGFSA RYYLVHQEPLENFQCNVPLGMESGRIANEQISASSTYSDGRWTPQQSRLHGDDNGWTPNL DSNKEYLQVDLRFLTMLTAIATQGAISRETQNGYYVKSYKLEVSTNGEDWMVYRHGKNHK VFQANNDATEVVLNKLHAPLLTRFVRIRPQTWHSGIALRLELFGCRVTDAPCSNMLGMLS GLIADSQISASSTQEYLWSPSAARLVSSRSGWFPRIPQAQPGEEWLQVDLGTPKTVKGVI IQGARGGDSITAVEARAFVRKFKVSYSLNGKDWEYIQDPRTQQPKLFEGNMHYDTPDIRR FDPIPAQYVRVYPERWSPAGIGMRLEVLGCDWTHHHHHH
>2QQK_2 Antibody Heavy Chain (chains H) EVQLVESGGGLVQPGGSLRLSCAASGFTISGYGIHWVRQAPGKGLEWVAYIYPDSGYTDY ADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCAREDFRNRRRLWYVMDYWGQGTLV TVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAV LQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTH
>2QQK_3 Antibody Light Chain (chains L) DIQMTQSPSSLSASVGDRVTITCRASQDVSTAVAWYQQKPGKAPKLLIYSASFLYSGVPS RFSGSGSGTDFTLTISSLQPEDFATYYCQQAWAYLPTFGQGTKVEIKRTVAAPSVFIFPP SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT LSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 2 |
Structural studies of neuropilin/antibody complexes provide insights into semaphorin and VEGF binding. Appleton, B.A., Wu, P., Maloney, J. et al. EMBO J (2007) 26:4902-4912. DOI 10.1038/sj.emboj.7601906 · PubMed
Other PDB entries of the same protein (UniProt O60462 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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