MolNFT v1 · #120310 · protein

Structure of tric-AMP-pnp

5GW5 · T-complex protein 1 subunit alpha: “Structure of tric-AMP-pnp”. Electron microscopy, 20 pockets (best druggability 0.86). MolNFT v1 #120310 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5GW5
Type: protein
Length: 8,446 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: P12612, P39076, P39078, P40413, P39077, P42943, P47079, P39079
Pockets: 20 · best druggability 0.86

Structure

electron microscopy · 8 distinct chains · 48% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
a, A	T-complex protein 1 subunit alpha	protein	543	46% helix, 15% strand	P12612
b, B	T-complex protein 1 subunit beta	protein	517	50% helix, 15% strand	P39076
d, D	T-complex protein 1 subunit delta	protein	521	48% helix, 16% strand	P39078
e, E	T-complex protein 1 subunit epsilon	protein	528	50% helix, 14% strand	P40413
g, G	T-complex protein 1 subunit gamma	protein	518	49% helix, 11% strand	P39077
h, H	T-complex protein 1 subunit eta	protein	519	49% helix, 16% strand	P42943
q, Q	T-complex protein 1 subunit theta	protein	543	46% helix, 14% strand	P47079
z, Z	T-complex protein 1 subunit zeta	protein	534	50% helix, 14% strand	P39079

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	1092	0.86	0.87	94	empty
2	897	0.85	0.87	96	empty
3	510	0.84	0.91	44	empty
4	968	0.84	0.85	94	empty
5	1084	0.84	0.85	139	empty

Interfaces

35 interfaces between chains.

E–H · 2452 Å² buried · 26 hydrogen bonds · protein-protein
e–h · 2311 Å² buried · 21 hydrogen bonds · protein-protein
B–E · 1989 Å² buried · 31 hydrogen bonds · protein-protein
b–e · 1940 Å² buried · 27 hydrogen bonds · protein-protein
q–z · 1904 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

5GW5 · Structure of TRiC-AMP-PNP · the same entry in another collection · chain Z against Z, 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 P12612
Every structure of UniProt P39076
Every structure of UniProt P39078
Every structure of UniProt P40413
Every structure of UniProt P39077
Every structure of UniProt P42943
Every structure of UniProt P47079
Every structure of UniProt P39079
Elsewhere: RCSB PDB 5GW5 · PDBe 5GW5 · UniProt P12612 · UniProt P39076 · UniProt P39078 · UniProt P40413 · UniProt P39077 · UniProt P42943 · UniProt P47079 · UniProt P39079

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