MolNFT v1 · #158354 · protein

Htric-hpfd CLASS1 (no pfd)

6NRA · T-complex protein 1 subunit alpha: “Htric-hpfd CLASS1 (no pfd)”. Electron microscopy, 20 pockets (best druggability 0.83). MolNFT v1 #158354 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6NRA
Type: protein
Length: 8,221 residues
Chains: 16
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: T-complex protein 1 subunit alpha; T-complex protein 1 subunit beta; T-complex protein 1…
UniProt: P17987, P78371, P49368, P50991, P48643, P40227, Q99832, P50990
Pockets: 20 · best druggability 0.83

Structure

electron microscopy · 15 distinct chains · 49% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	T-complex protein 1 subunit alpha	protein	521	46% helix, 12% strand	P17987
B	T-complex protein 1 subunit beta	protein	509	50% helix, 17% strand	P78371
C	T-complex protein 1 subunit gamma	protein	509	51% helix, 13% strand	P49368
D	T-complex protein 1 subunit delta	protein	508	50% helix, 14% strand	P50991
E, M	T-complex protein 1 subunit epsilon	protein	517	48% helix, 9% strand	P48643
F	T-complex protein 1 subunit zeta	protein	514	51% helix, 17% strand	P40227
G	T-complex protein 1 subunit eta	protein	512	47% helix, 13% strand	Q99832
H	T-complex protein 1 subunit theta	protein	510	47% helix, 12% strand	P50990
I	T-complex protein 1 subunit alpha	protein	534	45% helix, 12% strand	P17987
J	T-complex protein 1 subunit beta	protein	508	50% helix, 16% strand	P78371
K	T-complex protein 1 subunit gamma	protein	513	49% helix, 11% strand	P49368
L	T-complex protein 1 subunit delta	protein	513	48% helix, 11% strand	P50991
N	T-complex protein 1 subunit zeta	protein	513	51% helix, 15% strand	P40227
O	T-complex protein 1 subunit eta	protein	514	49% helix, 14% strand	Q99832
P	T-complex protein 1 subunit theta	protein	509	49% helix, 13% strand	P50990

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	291	0.83	0.93	48	empty
2	449	0.82	0.90	49	empty
3	920	0.82	0.83	84	empty
4	182	0.81	0.96	28	empty
5	183	0.81	0.97	39	empty

Interfaces

33 interfaces between chains.

M–O · 3857 Å² buried · 39 hydrogen bonds · protein-protein
E–G · 3798 Å² buried · 45 hydrogen bonds · protein-protein
I–K · 2377 Å² buried · 27 hydrogen bonds · protein-protein
J–L · 2215 Å² buried · 15 hydrogen bonds · protein-protein
I–L · 2144 Å² buried · 27 hydrogen bonds · protein-protein

Compared structures

6NRA · hTRiC-hPFD Class1 (No PFD) · 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 P17987
Every structure of UniProt P78371
Every structure of UniProt P49368
Every structure of UniProt P50991
Every structure of UniProt P48643
Every structure of UniProt P40227
Every structure of UniProt Q99832
Every structure of UniProt P50990
Elsewhere: RCSB PDB 6NRA · PDBe 6NRA · UniProt P17987 · UniProt P78371 · UniProt P49368 · UniProt P50991 · UniProt P48643 · UniProt P40227 · UniProt Q99832 · UniProt P50990

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