Research workbench

Cryo-EM structure of the yeast B*-A1 complex at an average resolution of 3.6 ångström

Analyse Cryo-EM structure of the yeast B*-A1 complex at an average resolution of 3.6… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6J6H
Type: protein + RNA
Length: 9,195 residues
Chains: 41
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P33334, P36048, Q03375, Q12417, P28004, P38241, Q12046, Q03772, P25337, P53333, Q03654, Q12309, P53277, P40968, P21374, Q04048, P40567, Q08963, Q06091, Q12330, Q02260, P40204, P54999, Q06217, P40018, P43321, P32523
Ligands: IHP, GTP, MG, ZN

Structure

electron microscopy · 37 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	1913	—	P33334
C	—	protein	920	—	P36048
J	—	protein	27	—	Q03375
O	—	protein	357	—	Q12417
P	—	protein	205	—	P28004
Q	—	protein	292	—	P38241
R	—	protein	261	—	Q12046
S	—	protein	70	—	Q03772
T	—	protein	157	—	P25337
Z	—	protein	447	—	P53333
c	—	protein	436	—	Q03654
d	—	protein	566	—	Q12309
I	—	protein	102	—	P53277
n	—	protein	23	—	P40968
H	—	protein	9	—	P21374
B	—	rna	60	—	—
D	—	rna	179	—	—
E	—	rna	103	—	—
L	—	rna	209	—	—
v	—	protein	722	—	Q04048
a	—	protein	84	—	P40567
b	—	protein	169	—	Q08963
t	—	protein	156	—	Q06091
u, i	—	protein	74	—	Q12330
m	—	protein	119	—	Q02260
j, x	—	protein	75	—	P40204
h, w	—	protein	68	—	P54999
g, e	—	protein	101	—	Q06217
k	—	protein	100	—	P40018
s	—	protein	93	—	P40018
l	—	protein	83	—	P43321
y	—	protein	81	—	P43321
z	—	protein	108	—	Q02260
r	—	protein	125	—	P32523
p	—	protein	128	—	P32523
q	—	protein	129	—	P32523
o	—	protein	126	—	P32523

Ligands and binding sites

IHP · Inositol hexakisphosphate · ligand · chains A
GTP · Guanosine-5'-triphosphate · ligand · chains A, C
MG · Magnesium ion · metal · 6 copies · chains C, E
ZN · Zinc ion · metal · 6 copies · chains Q, R, T

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

6J6H · Cryo-EM structure of the yeast B*-a1 complex at an average resolution of 3.6 angstrom · the same entry in another collection · chain c against c, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P33334
Every structure of UniProt P36048
Every structure of UniProt Q03375
Every structure of UniProt Q12417
Every structure of UniProt P28004
Every structure of UniProt P38241
Every structure of UniProt Q12046
Every structure of UniProt Q03772
Every structure of UniProt P25337
Every structure of UniProt P53333
Every structure of UniProt Q03654
Every structure of UniProt Q12309
Every structure of UniProt P53277
Every structure of UniProt P40968
Every structure of UniProt P21374
Every structure of UniProt Q04048
Every structure of UniProt P40567
Every structure of UniProt Q08963
Every structure of UniProt Q06091
Every structure of UniProt Q12330
Every structure of UniProt Q02260
Every structure of UniProt P40204
Every structure of UniProt P54999
Every structure of UniProt Q06217
Every structure of UniProt P40018
Every structure of UniProt P43321
Every structure of UniProt P32523
Elsewhere: RCSB PDB 6J6H · PDBe 6J6H · UniProt P33334 · UniProt P36048 · UniProt Q03375 · UniProt Q12417 · UniProt P28004 · UniProt P38241 · UniProt Q12046 · UniProt Q03772 · UniProt P25337 · UniProt P53333 · UniProt Q03654 · UniProt Q12309 · UniProt P53277 · UniProt P40968 · UniProt P21374 · UniProt Q04048 · UniProt P40567 · UniProt Q08963 · UniProt Q06091 · UniProt Q12330 · UniProt Q02260 · UniProt P40204 · UniProt P54999 · UniProt Q06217 · UniProt P40018 · UniProt P43321 · UniProt P32523

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