6H3C: BRISC complex
Cryo-EM structure of the BRISC complex bound to SHMT2. Determined by electron microscopy at 3.9 Å resolution. Released 10 Jul 2019.
- Method
- Electron microscopy
- Resolution
- 3.9 Å
- Organism
- Homo sapiens
- Chains
- 10
- Atoms
- 25,122
- Mol. weight
- 458.08 kDa
- Ligands
- ZN
- Released
- 10 Jul 2019
Explore 6H3C in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6H3C contains 144 α-helices and 134 β-strands across 10 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 and F: 8 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-5 | 4 | 1 |
| α-helix | 7-18 | 12 | |
| β-strand | 24-36 | 13 | 1 |
| β-strand | 50-61 | 12 | 1 |
| β-strand | 69-70 | 2 | 2 |
| β-strand | 74-75 | 2 | 2 |
| α-helix | 77-84 | 8 | |
| β-strand | 93-99 | 7 | 1 |
| α-helix | 107-119 | 13 | |
| β-strand | 126-134 | 9 | 1 |
| β-strand | 140-151 | 12 | 1 |
| β-strand | 154-157 | 4 | 1 |
| β-strand | 160-161 | 2 | 1 |
| α-helix | 165-167 | 3 | |
| α-helix | 176-180 | 5 | |
| α-helix | 183-191 | 9 | |
| α-helix | 193-195 | 3 | |
| α-helix | 204-254 | 51 | |
Chains B and G: 9 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 11-15 | 5 | 1 |
| α-helix | 16-26 | 11 | |
| β-strand | 36-44 | 9 | 1 |
| β-strand | 70-79 | 10 | 1 |
| α-helix | 94-111 | 18 | |
| β-strand | 116-124 | 9 | 1 |
| α-helix | 131-132 | 2 | |
| α-helix | 133-145 | 13 | |
| β-strand | 151-160 | 10 | 1 |
| β-strand | 165-175 | 11 | 1 |
| β-strand | 211-213 | 3 | 1 |
| β-strand | 216-219 | 4 | 1 |
| α-helix | 226-231 | 6 | |
| α-helix | 235-251 | 17 | |
| α-helix | 258-275 | 18 | |
| α-helix | 276-280 | 5 | |
| α-helix | 281-315 | 35 | |
Chains C and H: 20 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-8 | 6 | |
| α-helix | 15-23 | 9 | |
| β-strand | 36-41 | 6 | 3 |
| β-strand | 55-59 | 5 | 3 |
| β-strand | 62 | 1 | 4 |
| β-strand | 65 | 1 | 4 |
| β-strand | 70-72 | 3 | 3 |
| α-helix | 81-82 | 2 | |
| β-strand | 83-85 | 3 | 3 |
| α-helix | 87-89 | 3 | |
| α-helix | 100-103 | 4 | |
| α-helix | 110-112 | 3 | |
| α-helix | 113-132 | 20 | |
| α-helix | 136-138 | 3 | |
| α-helix | 139-143 | 5 | |
| α-helix | 144-146 | 3 | |
| α-helix | 149-153 | 5 | |
| β-strand | 156-159 | 4 | 5 |
| β-strand | 163 | 1 | 6 |
| β-strand | 168 | 1 | 6 |
| β-strand | 171-176 | 6 | 5 |
| α-helix | 184-186 | 3 | |
| β-strand | 201-207 | 7 | 5 |
| β-strand | 215 | 1 | 5 |
| β-strand | 218-221 | 4 | 5 |
| α-helix | 225-229 | 5 | |
| α-helix | 231-233 | 3 | |
| α-helix | 246-266 | 21 | |
| α-helix | 267-271 | 5 | |
| α-helix | 272-279 | 8 | |
| β-strand | 286-288 | 3 | 7 |
| β-strand | 296-301 | 6 | 7 |
| β-strand | 308-313 | 6 | 7 |
| β-strand | 324-333 | 10 | 7 |
| α-helix | 338 | 1 | |
| β-strand | 339-344 | 6 | 7 |
| α-helix | 355-373 | 19 | |
| α-helix | 374-379 | 6 | |
Chains D and I: 13 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 93-99 | 7 | 8 |
| α-helix | 103-106 | 4 | |
| β-strand | 110-111 | 2 | 9 |
| β-strand | 117-118 | 2 | 9 |
| α-helix | 120-134 | 15 | |
| β-strand | 143-148 | 6 | 8 |
| β-strand | 155-160 | 6 | 8 |
| α-helix | 163-170 | 8 | |
| β-strand | 181 | 1 | 10 |
| α-helix | 184-191 | 8 | |
| β-strand | 209-217 | 9 | 8 |
| α-helix | 220 | 1 | |
| β-strand | 221 | 1 | 10 |
| α-helix | 222 | 1 | |
| α-helix | 230-237 | 8 | |
| β-strand | 241-249 | 9 | 8 |
| α-helix | 251-254 | 4 | |
| α-helix | 260-268 | 9 | |
| α-helix | 269-271 | 3 | |
| β-strand | 279-283 | 5 | 8 |
| α-helix | 288-291 | 4 | |
| α-helix | 293-298 | 6 | |
| α-helix | 308-310 | 3 | |
Chains E and J: 22 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 28-31 | 4 | |
| α-helix | 33-47 | 15 | |
| β-strand | 50-51 | 2 | 21 |
| α-helix | 61-67 | 7 | |
| α-helix | 70-73 | 4 | |
| β-strand | 78 | 1 | 22 |
| β-strand | 83 | 1 | 22 |
| α-helix | 89-104 | 16 | |
| β-strand | 113-116 | 4 | 23 |
| α-helix | 119-120 | 2 | |
| β-strand | 121 | 1 | 24 |
| β-strand | 123 | 1 | 24 |
| α-helix | 125-133 | 9 | |
| β-strand | 139-142 | 4 | 23 |
| β-strand | 170-172 | 3 | 23 |
| β-strand | 176-177 | 2 | 25 |
| β-strand | 182-183 | 2 | 25 |
| α-helix | 185-195 | 11 | |
| β-strand | 199-203 | 5 | 23 |
| α-helix | 213-222 | 10 | |
| β-strand | 226-230 | 5 | 23 |
| α-helix | 235-239 | 5 | |
| α-helix | 246-248 | 3 | |
| β-strand | 252-256 | 5 | 23 |
| β-strand | 267-272 | 6 | 23 |
| β-strand | 275-279 | 5 | 26 |
| β-strand | 284-287 | 4 | 26 |
| α-helix | 291-294 | 4 | |
| α-helix | 295-297 | 3 | |
| α-helix | 308-321 | 14 | |
| α-helix | 324-346 | 23 | |
| β-strand | 350-351 | 2 | 27 |
| α-helix | 352-354 | 3 | |
| β-strand | 360-364 | 5 | 27 |
| α-helix | 366-368 | 3 | |
| α-helix | 372-380 | 9 | |
| β-strand | 384-385 | 2 | 21 |
| β-strand | 387-389 | 3 | 27 |
| β-strand | 402-406 | 5 | 27 |
| α-helix | 408-411 | 4 | |
| α-helix | 417-438 | 22 | |
| α-helix | 444-453 | 10 | |
| α-helix | 455-472 | 18 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| BRISC complex subunit Abraxas 2 | A, F | protein | 434 | Homo sapiens | Q15018 (AlphaFold model) |
| Lys-63-specific deubiquitinase BRCC36 | B, G | protein | 335 | Homo sapiens | P46736 (AlphaFold model) |
| BRISC and BRCA1-A complex member 2 | C, H | protein | 402 | Homo sapiens | Q9NXR7 (AlphaFold model) |
| BRISC and BRCA1-A complex member 1 | D, I | protein | 352 | Homo sapiens | Q9NWV8 (AlphaFold model) |
| Serine hydroxymethyltransferase, mitochondrial | E, J | protein | 507 | Homo sapiens | P34897 |
Sequence of entity 1 (A, F), FASTA
>6H3C_1 BRISC complex subunit Abraxas 2 (chains A, F)
MHHHHHHVDENLYFQGGGRMAASISGYTFSAVCFHSANSNADHEGFLLGEVRQEETFSIS
DSQISNTEFLQVIEIHNHQPCSKLFSFYDYASKVNEESLDRILKDRRKKVIGWYRFRRNT
QQQMSYREQVLHKQLTRILGVPDLVFLLFSFISTANNSTHALEYVLFRPNRRYNQRISLA
IPNLGNTSQQEYKVSSVPNTSQSYAKVIKEHGTDFFDKDGVMKDIRAIYQVYNALQEKVQ
AVCADVEKSERVVESCQAEVNKLRRQITQRKNEKEQERRLQQAVLSRQMPSESLDPAFSP
RMPSSGFAAEGRSTLGDAEASDPPPPYSDFHPNNQESTLSHSRMERSVFMPRPQAVGSSN
YASTSAGLKYPGSGADLPPPQRAAGDSGEDSDDSDYENLIDPTEPSNSEYSHSKDSRPMA
HPDEDPRNTQTSQI
Sequence of entity 2 (B, G), FASTA
>6H3C_2 Lys-63-specific deubiquitinase BRCC36 (chains B, G)
MHHHHHHVDENLYFQGGGRMAVQVVQAVQAVHLESDAFLVCLNHALSTEKEEVMGLCIGE
LNDDTRSDSKFAYTGTEMRTVAEKVDAVRIVHIHSVIILRRSDKRKDRVEISPEQLSAAS
TEAERLAELTGRPMRVVGWYHSHPHITVWPSHVDVRTQAMYQMMDQGFVGLIFSCFIEDK
NTKTGRVLYTCFQSIQAQKSSESLHGPRDFWSSSQHISIEGQKEEERYERIEIPIHIVPH
VTIGKVCLESAVELPKILCQEEQDAYRRIHSLTHLDSVTKIHNGSVFTKNLCSQMSAVSG
PLLQWLEDRLEQNQQHLQELQQEKEELMQELSSLE
Sequence of entity 3 (C, H), FASTA
>6H3C_3 BRISC and BRCA1-A complex member 2 (chains C, H)
MHHHHHHVDENLYFQGGGRMSPEVALNRISPMLSPFISSVVRNGKVGLDATNCLRITDLK
SGCTSLTPGPNCDRFKLHIPYAGETLKWDIIFNAQYPELPPDFIFGEDAEFLPDPSALQN
LASWNPSNPECLLLVVKELVQQYHQFQCSRLRESSRLMFEYQTLLEEPQYGENMEIYAGK
KNNWTGEFSARFLLKLPVDFSNIPTYLLKDVNEDPGEDVALLSVSFEDTEATQVYPKLYL
SPRIEHALGGSSALHIPAFPGGGCLIDYVPQVCHLLTNKVQYVIQGYHKRREYIAAFLSH
FGTGVVEYDAEGFTKLTLLLMWKDFCFLVHIDLPLFFPRDQPTLTFQSVYHFTNSGQLYS
QAQKNYPYSPRWDGNEMAKRAKAYFKTFVPQFQEAAFANGKL
Sequence of entity 4 (D, I), FASTA
>6H3C_4 BRISC and BRCA1-A complex member 1 (chains D, I)
MASWSHPQFEKVDENLYFQGGGRMEVAEPSSPTEEEEEEEEHSAEPRPRTRSNPEGAEDR
AVGAQASVGSRSEGEGEAASADDGSLNTSGAGPKSWQVPPPAPEVQIRTPRVNCPEKVII
CLDLSEEMSLPKLESFNGSKTNALNVSQKMIEMFVRTKHKIDKSHEFALVVVNDDTAWLS
GLTSDPRELCSCLYDLETASCSTFNLEGLFSLIQQKTELPVTENVQTIPPPYVVRTILVY
SRPPCQPQFSLTEPMKKMFQCPYFFFDVVYIHNGTEEKEEEMSWKDMFAFMGSLDTKGTS
YKYEVALAGPALELHNCMAKLLAHPLQRPCQSHASYSLLEEEDEAIEVEATV
Sequence of entity 5 (E, J), FASTA
>6H3C_5 Serine hydroxymethyltransferase, mitochondrial (chains E, J)
MGSSHHHHHHSSGLVPRGSGQLVRMAIRAQHSNAAQTQTGEANRGWTGQESLSDSDPEMW
ELLQREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIEL
LCQRRALEAFDLDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYM
SDVKRISATSIFFESMPYKLNPKTGLIDYNQLALTARLFRPRLIIAGTSAYARLIDYARM
REVCDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRGTRSGLIFYRKGVK
AVDPKTGREIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKN
ARAMADALLERGYSLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRS
AITPGGLRLGAPALTSRQFREDDFRRVVDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSE
TSQRLANLRQRVEQFARAFPMPGFDEH
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ZN | Zinc ion | Zn | 2 |
Primary citation
Structural Basis of BRCC36 Function in DNA Repair and Immune Regulation. Rabl, J., Bunker, R.D., Schenk, A.D. et al. Mol Cell (2019) 75:483-497.e9. DOI 10.1016/j.molcel.2019.06.002 · PubMed
Other PDB entries of the same protein (UniProt Q15018 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 8PVY 3.02 Å, Cryo-EM structure of the human BRISC dimer complex bound to compound FX-171-C
- 8PY2 3.32 Å, Cryo-EM structure of the human BRISC dimer complex bound to compound JMS-175-2
- 6R8F 3.8 Å, Cryo-EM structure of the Human BRISC-SHMT2 complex
Browse structure collections
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