MolNFT v1 · #93031 · protein

The conformations and interactions of the four-layer aggregate revealed by X-ray crystallography diffraction implied the importance of peptides at opposite ends in their assemblies

4GQH: “The conformations and interactions of the four-layer aggregate revealed by X-ray crystallography diffraction…”. X-ray diffraction. MolNFT v1 #93031 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4GQH
Type: protein
Length: 4,690 residues
Chains: 34
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P69687

Structure

x-ray diffraction · 20 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	142	—	P69687
B	—	protein	139	—	P69687
C	—	protein	144	—	P69687
D	—	protein	143	—	P69687
E, O	—	protein	140	—	P69687
F, K	—	protein	143	—	P69687
G	—	protein	143	—	P69687
H	—	protein	144	—	P69687
I, L	—	protein	141	—	P69687
J	—	protein	145	—	P69687
M, N	—	protein	142	—	P69687
P	—	protein	147	—	P69687
Q	—	protein	146	—	P69687
R, S, U	—	protein	133	—	P69687
T	—	protein	132	—	P69687
V, W, Z, d, e, f, h, i	—	protein	134	—	P69687
X	—	protein	131	—	P69687
Y, b	—	protein	132	—	P69687
a	—	protein	131	—	P69687
c	—	protein	136	—	P69687

Compared structures

4GQH · The Conformations and Interactions of the Four-Layer Aggregate Revealed by X-ray… · the same entry in another collection · chain B against B, 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 P69687
Elsewhere: RCSB PDB 4GQH · PDBe 4GQH · UniProt P69687

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