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Cyanophage PAM1 portal-adaptor complex

Analyse Cyanophage PAM1 portal-adaptor complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7EEP
Type: protein
Length: 8,532 residues
Chains: 24
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: PAM1 portal proteins; PAM1 adaptor proteins
Pockets: 20 · best druggability 0.84

Structure

electron microscopy · 2 distinct chains · 30% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L	PAM1 portal proteins	protein	529	30% helix, 12% strand	—
M, N, O, P, Q, R, S, T, U, V, W, X	PAM1 adaptor proteins	protein	182	27% helix, 16% strand	—

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	1060	0.84	0.85	120	empty
2	1072	0.84	0.85	110	empty
3	1077	0.84	0.85	108	empty
4	1038	0.84	0.85	107	empty
5	1090	0.84	0.85	113	empty

Interfaces

60 interfaces between chains.

F–G · 6325 Å² buried · 64 hydrogen bonds · protein-protein
I–J · 6315 Å² buried · 61 hydrogen bonds · protein-protein
A–B · 6309 Å² buried · 62 hydrogen bonds · protein-protein
E–F · 6309 Å² buried · 61 hydrogen bonds · protein-protein
B–C · 6309 Å² buried · 62 hydrogen bonds · protein-protein

Compared structures

7EEP · Cyanophage Pam1 portal-adaptor complex · the same entry in another collection · chain A against A, 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
Elsewhere: RCSB PDB 7EEP · PDBe 7EEP

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