3RSE: Actin-related protein 3
Structural and biochemical characterization of two binding sites for nucleation promoting factor WASp-VCA on Arp2/3 complex. Determined by X-ray diffraction at 2.65 Å resolution. Released 1 Jun 2011.
- Method
- X-ray diffraction
- Resolution
- 2.65 Å
- Organism
- Bos taurus
- Chains
- 8
- Atoms
- 13,807
- Mol. weight
- 224.66 kDa
- Released
- 1 Jun 2011
Explore 3RSE in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3RSE contains 84 α-helices and 80 β-strands across 7 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: 27 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-7 | 2 | |
| β-strand | 8-12 | 5 | 1 |
| β-strand | 16-21 | 6 | 1 |
| β-strand | 29-32 | 4 | 1 |
| β-strand | 35-37 | 3 | 2 |
| α-helix | 56-58 | 3 | |
| β-strand | 61-62 | 2 | 2 |
| α-helix | 63-66 | 4 | |
| β-strand | 73-75 | 3 | 2 |
| β-strand | 78-79 | 2 | 3 |
| β-strand | 82-83 | 2 | 3 |
| α-helix | 86-95 | 10 | |
| α-helix | 96-101 | 6 | |
| α-helix | 105-107 | 3 | |
| β-strand | 110-114 | 5 | 1 |
| α-helix | 120-127 | 8 | |
| α-helix | 128-133 | 6 | |
| β-strand | 138-143 | 6 | 1 |
| α-helix | 144-152 | 9 | |
| β-strand | 165-170 | 6 | 4 |
| β-strand | 175-181 | 7 | 4 |
| β-strand | 184-185 | 2 | 4 |
| α-helix | 187-189 | 3 | |
| β-strand | 191-193 | 3 | 4 |
| α-helix | 197-209 | 13 | |
| α-helix | 217-219 | 3 | |
| α-helix | 220-231 | 12 | |
| α-helix | 238-247 | 10 | |
| α-helix | 249-252 | 4 | |
| β-strand | 254-257 | 4 | 5 |
| β-strand | 268-271 | 4 | 5 |
| α-helix | 274-277 | 4 | |
| α-helix | 279-282 | 4 | |
| α-helix | 285-287 | 3 | |
| α-helix | 296-306 | 11 | |
| α-helix | 309-317 | 9 | |
| β-strand | 319-322 | 4 | 4 |
| α-helix | 324-327 | 4 | |
| α-helix | 331-351 | 21 | |
| α-helix | 360-363 | 4 | |
| β-strand | 367-368 | 2 | 4 |
| α-helix | 376-385 | 10 | |
| α-helix | 388-393 | 6 | |
| β-strand | 395-396 | 2 | 1 |
| α-helix | 397-403 | 7 | |
| α-helix | 405-409 | 5 | |
Chain B: 12 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 155-159 | 5 | 6 |
| β-strand | 164-168 | 5 | 6 |
| β-strand | 169-170 | 2 | 7 |
| β-strand | 173-174 | 2 | 7 |
| β-strand | 180-182 | 3 | 6 |
| α-helix | 186-199 | 14 | |
| α-helix | 210-220 | 11 | |
| α-helix | 227-236 | 10 | |
| β-strand | 242-245 | 4 | 8 |
| β-strand | 251-254 | 4 | 8 |
| α-helix | 257-260 | 4 | |
| α-helix | 261-266 | 6 | |
| α-helix | 268-271 | 4 | |
| α-helix | 278-286 | 9 | |
| α-helix | 294-297 | 4 | |
| β-strand | 302-304 | 3 | 6 |
| α-helix | 306-308 | 3 | |
| α-helix | 313-324 | 12 | |
| α-helix | 325-329 | 5 | |
| α-helix | 337-339 | 3 | |
Chain C: 4 helices, 30 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-5 | 3 | 9 |
| β-strand | 13-16 | 4 | 10 |
| β-strand | 22-26 | 5 | 10 |
| β-strand | 31-38 | 8 | 10 |
| β-strand | 41-49 | 9 | 10 |
| β-strand | 55-61 | 7 | 11 |
| β-strand | 66-71 | 6 | 11 |
| β-strand | 76-82 | 7 | 11 |
| β-strand | 85-91 | 7 | 11 |
| β-strand | 99-104 | 6 | 12 |
| β-strand | 110-115 | 6 | 12 |
| β-strand | 120-126 | 7 | 12 |
| β-strand | 131-137 | 7 | 12 |
| β-strand | 145-150 | 6 | 13 |
| β-strand | 156-161 | 6 | 13 |
| β-strand | 166-170 | 5 | 13 |
| β-strand | 183 | 1 | 14 |
| β-strand | 186 | 1 | 14 |
| β-strand | 194-197 | 4 | 13 |
| β-strand | 205-210 | 6 | 15 |
| β-strand | 216-221 | 6 | 15 |
| β-strand | 225-230 | 6 | 15 |
| α-helix | 231-233 | 3 | |
| β-strand | 236-241 | 6 | 15 |
| α-helix | 245-246 | 2 | |
| β-strand | 247-254 | 8 | 16 |
| β-strand | 257-262 | 6 | 16 |
| β-strand | 268-273 | 6 | 16 |
| β-strand | 278-281 | 4 | 16 |
| α-helix | 298-303 | 6 | |
| β-strand | 329-336 | 8 | 9 |
| β-strand | 344-349 | 6 | 9 |
| β-strand | 353-358 | 6 | 9 |
| α-helix | 359-365 | 7 | |
Chain D: 16 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-5 | 2 | |
| α-helix | 9-24 | 16 | |
| α-helix | 26-30 | 5 | |
| β-strand | 32-36 | 5 | 17 |
| β-strand | 42-46 | 5 | 17 |
| α-helix | 48-50 | 3 | |
| β-strand | 54-60 | 7 | 17 |
| α-helix | 64-68 | 5 | |
| α-helix | 72-80 | 9 | |
| α-helix | 81-83 | 3 | |
| β-strand | 84-85 | 2 | 17 |
| β-strand | 93-98 | 6 | 17 |
| α-helix | 107-114 | 8 | |
| α-helix | 116-133 | 18 | |
| α-helix | 139-141 | 3 | |
| β-strand | 142-147 | 6 | 18 |
| β-strand | 150-156 | 7 | 18 |
| β-strand | 161-168 | 8 | 18 |
| α-helix | 172-185 | 14 | |
| α-helix | 188-191 | 4 | |
| α-helix | 196 | 1 | |
| β-strand | 197-202 | 6 | 18 |
| β-strand | 220-227 | 8 | 18 |
| α-helix | 229-232 | 4 | |
| α-helix | 237-244 | 8 | |
| α-helix | 247-279 | 33 | |
Chain E: 8 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 14 | 1 | 19 |
| β-strand | 21 | 1 | 19 |
| α-helix | 41-52 | 12 | |
| α-helix | 63-82 | 20 | |
| α-helix | 87-100 | 14 | |
| α-helix | 118-120 | 3 | |
| α-helix | 123-148 | 26 | |
| β-strand | 149 | 1 | 20 |
| β-strand | 156 | 1 | 20 |
| α-helix | 158-161 | 4 | |
| α-helix | 162-165 | 4 | |
| α-helix | 168-170 | 3 | |
Chain F: 8 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-19 | 15 | |
| α-helix | 37-40 | 4 | |
| α-helix | 44-46 | 3 | |
| β-strand | 47 | 1 | 21 |
| β-strand | 51-54 | 4 | 22 |
| β-strand | 60-65 | 6 | 22 |
| β-strand | 66 | 1 | 21 |
| β-strand | 69-75 | 7 | 22 |
| α-helix | 81-95 | 15 | |
| α-helix | 98-101 | 4 | |
| β-strand | 104 | 1 | 22 |
| α-helix | 108-109 | 2 | |
| β-strand | 114-119 | 6 | 22 |
| α-helix | 120-125 | 6 | |
| α-helix | 128-165 | 38 | |
Chain G: 9 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-13 | 3 | |
| α-helix | 16-19 | 4 | |
| α-helix | 39-47 | 9 | |
| α-helix | 51-58 | 8 | |
| α-helix | 69-85 | 17 | |
| α-helix | 88-90 | 3 | |
| α-helix | 91-96 | 6 | |
| α-helix | 100-113 | 14 | |
| β-strand | 118 | 1 | 23 |
| β-strand | 120 | 1 | 23 |
| α-helix | 121-146 | 26 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Actin-related protein 3 | A | protein | 418 | Bos taurus | P61157 (AlphaFold model) |
| Actin-related protein 2 | B | protein | 394 | Bos taurus | A7MB62 (AlphaFold model) |
| Actin-related protein 2/3 complex subunit 1B | C | protein | 372 | Bos taurus | Q58CQ2 (AlphaFold model) |
| Actin-related protein 2/3 complex subunit 2 | D | protein | 300 | Bos taurus | Q3MHR7 (AlphaFold model) |
| Actin-related protein 2/3 complex subunit 3 | E | protein | 178 | Bos taurus | Q3T035 |
| Actin-related protein 2/3 complex subunit 4 | F | protein | 168 | Bos taurus | Q148J6 |
| Actin-related protein 2/3 complex subunit 5 | G | protein | 151 | Bos taurus | Q3SYX9 |
| CA fragment of Bos taurus N-WASP | Z | protein | 3 | Bos taurus | Q95107 |
Sequence of entity 1 (A), FASTA
>3RSE_1 Actin-related protein 3 (chains A)
MAGRLPACVVDCGTGYTKLGYAGNTEPQFIIPSCIAIKESAKVGDQAQRRVMKGVDDLDF
FIGDEAIEKPTYATKWPIRHGIVEDWDLMERFMEQVIFKYLRAEPEDHYFLLTEPPLNTP
ENREYTAEIMFESFNVPGLYIAVQAVLALAASWTSRQVGERTLTGTVIDSGDGVTHVIPV
AEGYVIGSCIKHIPIAGRDITYFIQQLLRDREVGIPPEQSLETAKAVKERYSYVCPDLVK
EFNKYDTDGSKWIKQYTGINAISKKEFSIDVGYERFLGPEIFFHPEFANPDFTQPISEVV
DEVIQNCPIDVRRPLYKNIVLSGGSTMFRDFGRRLQRDLKRTVDARLKLSEELSGGRLKP
KPIDVQVITHHMQRYAVWFGGSMLASTPEFYQVCHTKKDYEEIGPSICRHNPVFGVMS
Sequence of entity 2 (B), FASTA
>3RSE_2 Actin-related protein 2 (chains B)
MDSQGRKVVVCDNGTGFVKCGYAGSNFPEHIFPALVGRPIIRSTTKVGNIEIKDLMVGDE
ASELRSMLEVNYPMENGIVRNWDDMKHLWDYTFGPEKLNIDTRNCKILLTEPPMNPTKNR
EKIVEVMFETYQFSGVYVAIQAVLTLYAQGLLTGVVVDSGDGVTHICPVYEGFSLPHLTR
RLDIAGRDITRYLIKLLLLRGYAFNHSADFETVRMIKEKLCYVGYNIEQEQKLALETTVL
VESYTLPDGRIIKVGGERFEAPEALFQPHLINVEGVGVAELLFNTIQAADIDTRSEFYKH
IVLSGGSTMYPGLPSRLERELKQLYLERVLKGDVEKLSKFKIRIEDPPRRKHMVFLGGAV
LADIMKDKDNFWMTRQEYQEKGVRVLEKLGVTVR
Sequence of entity 3 (C), FASTA
>3RSE_3 Actin-related protein 2/3 complex subunit 1B (chains C)
MAYHSFLVEPISCHAWNKDRTQIAICPNNHEVHIYEKSGNKWVQVHELKEHNGQVTGIDW
APDSNRIVTCGTDRNAYVWTLKGRTWKPTLVILRINRAARCVRWAPNEKKFAVGSGSRVI
SICYFEQENDWWVCKHIKKPIRSTVLSLDWHPNSVLLAAGSCDFKCRIFSAYIKEVEERP
APTPWGSKMPFGELMFESSSSCGWVHGVCFSANGSRVAWVSHDSTVCLADADKKMAVATL
ASETLPLLAVTFITESSLVAAGHDCFPVLFTYDSAAGKLSFGGRLDVPKQSSQRGLTARE
RFQNLDKKASSEGSAAAGAGLDSLHKNSVSQISVLSGGKAKCSQFCTTGMDGGMSIWDVR
SLESALKDLKIV
Sequence of entity 4 (D), FASTA
>3RSE_4 Actin-related protein 2/3 complex subunit 2 (chains D)
MILLEVNNRIIEETLALKFENAAAGNKPEAVEVTFADFDGVLYHISNPNGDKTKVMVSIS
LKFYKELQAHGADELLKRVYGSYLVNPESGYNVSLLYDLENLPASKDSIVHQAGMLKRNC
FASVFEKYFQFQEEGKEGENRAVIHYRDDETMYVESKKDRVTVVFSTVFKDDDDVVIGKV
FMQEFKEGRRASHTAPQVLFSHREPPLELKDTDAAVGDNIGYITFVLFPRHTNASARDNT
INLIHTFRDYLHYHIKCSKAYIHTRMRAKTSDFLKVLNRARPDAEKKEMKTITGKTFSSR
Sequence of entity 5 (E), FASTA
>3RSE_5 Actin-related protein 2/3 complex subunit 3 (chains E)
MPAYHSSLMDPDTKLIGNMALLPIRSQFKGPAPRETKDTDIVDEAIYYFKANVFFKNYEI
KNEADRTLIYITLYISECLKKLQKCNSKSQGEKEMYTLGITNFPIPGEPGFPLNAIYAKP
ANKQEDEVMRAYLQQLRQETGLRLCEKVFDPQNDKPSKWWTCFVKRQFMNKSLSGPGQ
Sequence of entity 6 (F), FASTA
>3RSE_6 Actin-related protein 2/3 complex subunit 4 (chains F)
MTATLRPYLSAVRATLQAALCLENFSSQVVERHNKPEVEVRSSKELLLQPVTISRNEKEK
VLIEGSINSVRVSIAVKQADEIEKILCHKFMRFMMMRAENFFILRRKPVEGYDISFLITN
FHTEQMYKHKLVDFVIHFMEEIDKEISEMKLSVNARARIVAEEFLKNF
Sequence of entity 7 (G), FASTA
>3RSE_7 Actin-related protein 2/3 complex subunit 5 (chains G)
MSKNTVSSARFRKVDVGEYDENKFVDEEDGGDGQAGPDEGEVDSCLRQGNMTAALQAALK
NPPINTKSQAVKDRAGSIVLKVLISFKANDIEKAVQSLDKNGVDLLMKYIYKGFESPSDN
SSAVLLQWHEKALAAGGVGSIVRVLTARKTV
Sequence of entity 8 (Z), FASTA
>3RSE_8 CA fragment of Bos taurus N-WASP (chains Z)
EWE
Primary citation
Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASp-VCA on Arp2/3 complex. Ti, S.C., Jurgenson, C.T., Nolen, B.J. et al. Proc Natl Acad Sci U S A (2011) 108:E463-E471. DOI 10.1073/pnas.1100125108 · PubMed
Other PDB entries of the same protein (UniProt P61157 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 1K8K 2.0 Å, Crystal Structure of Arp2/3 Complex
- 2P9I 2.46 Å, Crystal Structure of bovine Arp2/3 Complex co-crystallized with ADP and crosslinked with…
- 3UKR 2.48 Å, Crystal structure of Bos taurus Arp2/3 complex with bound inhibitor CK-666
- 3ULE 2.5 Å, Structure of Bos taurus Arp2/3 complex with bound inhibitor CK-869 and ATP
- 1TYQ 2.55 Å, Crystal structure of Arp2/3 complex with bound ATP and calcium
- 1U2V 2.55 Å, Crystal structure of Arp2/3 complex with bound ADP and calcium
- 2P9K 2.59 Å, Crystal structure of bovine Arp2/3 complex co-crystallized with ATP and crosslinked with…
- 2P9L 2.65 Å, Crystal Structure of bovine Arp2/3 complex
- 2P9S 2.68 Å, Structure of bovine Arp2/3 complex co-crystallized with ATP/Mg2+
- 3DXK 2.7 Å, Structure of Bos Taurus Arp2/3 Complex with Bound Inhibitor CK0944636
- 2P9U 2.75 Å, Crystal structure of bovine Arp2/3 complex co-crystallized with AMP-PNP and calcium
- 3UKU 2.75 Å, Structure of Arp2/3 complex with bound inhibitor CK-869
Browse structure collections
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