6R8F: Human BRISC-SHMT2 complex

Cryo-EM structure of the Human BRISC-SHMT2 complex. Determined by electron microscopy at 3.8 Å resolution. Released 5 Jun 2019.

Method: Electron microscopy
Resolution: 3.8 Å
Organism: Homo sapiens
Chains: 8
Atoms: 15,810
Mol. weight: 290.69 kDa
Ligands: ZN
Released: 5 Jun 2019

Explore 6R8F in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6R8F contains 82 α-helices and 90 β-strands across 8 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 C: 8 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	11-15	5	1
α-helix	16-26	11
β-strand	35-42	8	1
β-strand	71-79	9	1
α-helix	94-111	18
β-strand	116-123	8	1
α-helix	133-140	8
β-strand	152-158	7	1
β-strand	166-172	7	1
β-strand	174	1	2
β-strand	212	1	2
β-strand	216-219	4	1
α-helix	227-230	4
α-helix	234-249	16
α-helix	260-263	4
α-helix	268-271	4
α-helix	284-310	27

Chains B and D: 8 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	4-5	2	1
α-helix	9-16	8
β-strand	24-32	9	1
β-strand	52-58	7	1
α-helix	74-76	3
α-helix	77-80	4
β-strand	91-97	7	1
α-helix	108-110	3
α-helix	113-119	7
β-strand	126-131	6	1
β-strand	134	1	1
β-strand	140-146	7	1
β-strand	161	1	1
α-helix	183-192	10
α-helix	193-195	3
α-helix	210-251	42

Chains E and G: 5 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	12-14	3
α-helix	16-24	9
β-strand	37-38	2	15
β-strand	56-60	5	15
β-strand	67-72	6	15
β-strand	83-86	4	15
α-helix	112-129	18
α-helix	141-148	8
β-strand	160-163	4	16
β-strand	175-178	4	16
β-strand	179-180	2	17
β-strand	202-203	2	17
β-strand	207	1	16
β-strand	218	1	17
α-helix	243-254	12

Chains K and L: 20 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	49-52	4
α-helix	54-68	15
β-strand	71-72	2	3
α-helix	78-81	4
α-helix	82-84	3
α-helix	115-124	10
β-strand	134-136	3	4
β-strand	139	1	4
α-helix	151-154	4
β-strand	160-164	5	4
β-strand	191-195	5	4
β-strand	197	1	5
β-strand	204	1	5
α-helix	208-216	9
β-strand	220-222	3	4
α-helix	236-243	8
β-strand	247-250	4	4
α-helix	267-269	3
β-strand	273-277	5	4
β-strand	288-293	6	4
β-strand	296-297	2	6
β-strand	307-308	2	6
α-helix	312-315	4
α-helix	316-318	3
α-helix	330-333	4
α-helix	340-343	4
α-helix	345-368	24
β-strand	371-372	2	7
β-strand	383-385	3	7
α-helix	394-400	7
α-helix	401-403	3
β-strand	405-406	2	3
β-strand	409-410	2	7
β-strand	423-425	3	7
α-helix	430-433	4
α-helix	438-461	24
α-helix	465-471	7
α-helix	476-492	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Lys-63-specific deubiquitinase BRCC36	A, C	protein	316	Homo sapiens	P46736 (AlphaFold model)
BRISC complex subunit Abraxas 2	B, D	protein	267	Homo sapiens	Q15018 (AlphaFold model)
Serine hydroxymethyltransferase, mitochondrial	K, L	protein	504	Homo sapiens	P34897 (AlphaFold model)
BRISC and BRCA1-A complex member 2,BRCC45 (BRE, BRISC and BRCA1-A complex member 2)	E, G	protein	217	Homo sapiens	Q9NXR7 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>6R8F_1 Lys-63-specific deubiquitinase BRCC36 (chains A, C)
MAVQVVQAVQAVHLESDAFLVCLNHALSTEKEEVMGLCIGELNDDTRSDSKFAYTGTEMR
TVAEKVDAVRIVHIHSVIILRRSDKRKDRVEISPEQLSAASTEAERLAELTGRPMRVVGW
YHSHPHITVWPSHVDVRTQAMYQMMDQGFVGLIFSCFIEDKNTKTGRVLYTCFQSIQAQK
SSESLHGPRDFWSSSQHISIEGQKEEERYERIEIPIHIVPHVTIGKVCLESAVELPKILC
QEEQDAYRRIHSLTHLDSVTKIHNGSVFTKNLCSQMSAVSGPLLQWLEDRLEQNQQHLQE
LQQEKEELMQELSSLE

Sequence of entity 2 (B, D), FASTA

>6R8F_2 BRISC complex subunit Abraxas 2 (chains B, D)
MAASISGYTFSAVCFHSANSNADHEGFLLGEVRQEETFSISDSQISNTEFLQVIEIHNHQ
PCSKLFSFYDYASKVNEESLDRILKDRRKKVIGWYRFRRNTQQQMSYREQVLHKQLTRIL
GVPDLVFLLFSFISTANNSTHALEYVLFRPNRRYNQRISLAIPNLGNTSQQEYKVSSVPN
TSQSYAKVIKEHGTDFFDKDGVMKDIRAIYQVYNALQEKVQAVCADVEKSERVVESCQAE
VNKLRRQITQRKNEKEQERRLQQAVLS

Sequence of entity 3 (K, L), FASTA

>6R8F_3 Serine hydroxymethyltransferase, mitochondrial (chains K, L)
MLYFSLFWAARPLQRCGQLVRMAIRAQHSNAAQTQTGEANRGWTGQESLSDSDPEMWELL
QREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQ
RRALEAFDLDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDV
KRISATSIFFESMPYKLNPKTGLIDYNQLALTARLFRPRLIIAGTSAYARLIDYARMREV
CDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRGTRSGLIFYRKGVKAVD
PKTGREIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARA
MADALLERGYSLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAIT
PGGLRLGAPALTSRQFREDDFRRVVDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQ
RLANLRQRVEQFARAFPMPGFDEH

Sequence of entity 4 (E, G), FASTA

>6R8F_4 BRISC and BRCA1-A complex member 2,BRCC45 (BRE, BRISC and BRCA1-A complex member 2) (chains E, G)
GAMSPEVALNRISPMLSPFISSVVRNGKVGLDATNCLRITDLKSGCTSLTPGPNCDRFKL
HIPYAGETLKWDIIFNAQYPELPPDFIFGEDAEFLPDPSALQNLASWNPSNPECLLLVVK
ELVQQYHQFQCSRLRXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	2

Primary citation

Metabolic control of BRISC-SHMT2 assembly regulates immune signalling. Walden, M., Tian, L., Ross, R.L. et al. Nature (2019) 570:194-199. DOI 10.1038/s41586-019-1232-1 · PubMed

Other PDB entries of the same protein (UniProt P46736 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9SQY 2.92 Å, Cryo-EM structure of the ARISC(E33A)-RAP80:K63-Ub7 complex (Composite map)
9SMP 3.0 Å, BRCA1-A complex bound to K63-polyUbATA - open form double State P
8PVY 3.02 Å, Cryo-EM structure of the human BRISC dimer complex bound to compound FX-171-C
9SMN 3.2 Å, BRCA1-A complex bound to K63-polyUbATA - open form StateC StateP
9SNA 3.2 Å, BRCA1-A complex bound to K63-diUbATA - open form StateC StateP
9SQW 3.2 Å, Cryo-EM structure of the ARISCdC(E33A):K63-Ub7 complex (Composite map)
9SQV 3.21 Å, Cryo-EM structure of the ARISCdC(E33A):K63-Ub4 complex (Composite map)
9SMR 3.25 Å, Structure of apo BRCA1-A complex in presence of K63-oligoUbATA
8PY2 3.32 Å, Cryo-EM structure of the human BRISC dimer complex bound to compound JMS-175-2
9SO9 3.4 Å, BRCA1-A complex bound to K63-oligoUbATA - closed form StateC*
6H3C 3.9 Å, Cryo-EM structure of the BRISC complex bound to SHMT2

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