MolNFT v1 · #73849 · protein

Structure of four mutant forms of yeast F1 ATPase: beta-V279F

3OEH: “Structure of four mutant forms of yeast F1 ATPase: beta-V279F”. X-ray diffraction. MolNFT v1 #73849 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3OEH
Type: protein
Length: 9,597 residues
Chains: 27
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P07251, P00830, P38077, Q12165, P21306

Structure

x-ray diffraction · 22 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, L	—	protein	482	—	P07251
B	—	protein	483	—	P07251
C	—	protein	484	—	P07251
D, M, N, V	—	protein	470	—	P00830
E	—	protein	468	—	P00830
F, X	—	protein	469	—	P00830
G	—	protein	266	—	P38077
H	—	protein	116	—	Q12165
I	—	protein	49	—	P21306
J	—	protein	481	—	P07251
K	—	protein	486	—	P07251
O	—	protein	468	—	P00830
P	—	protein	246	—	P38077
Q	—	protein	84	—	Q12165
R	—	protein	34	—	P21306
S	—	protein	478	—	P07251
T	—	protein	479	—	P07251
U	—	protein	481	—	P07251
W	—	protein	467	—	P00830
Y	—	protein	201	—	P38077
Z	—	protein	17	—	Q12165
1	—	protein	27	—	P21306

Compared structures

3OEH · Structure of four mutant forms of yeast F1 ATPase: beta-V279F · the same entry in another collection · chain J against J, 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 P07251
Every structure of UniProt P00830
Every structure of UniProt P38077
Every structure of UniProt Q12165
Every structure of UniProt P21306
Elsewhere: RCSB PDB 3OEH · PDBe 3OEH · UniProt P07251 · UniProt P00830 · UniProt P38077 · UniProt Q12165 · UniProt P21306

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