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H57A hfq from pseudomonas aeruginosa

Analyse H57A hfq from pseudomonas aeruginosa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3M4G
Type: protein
Length: 826 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein hfq
UniProt: Q9HUM0
Ligands: ZN
Pockets: 5 · best druggability 0.81

Structure

x-ray diffraction · 8 distinct chains · 19% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein hfq	protein	68	19% helix, 46% strand	Q9HUM0
B, H	Protein hfq	protein	69	19% helix, 43% strand	Q9HUM0
C, L	Protein hfq	protein	70	19% helix, 43% strand	Q9HUM0
D	Protein hfq	protein	66	20% helix, 45% strand	Q9HUM0
E	Protein hfq	protein	70	19% helix, 43% strand	Q9HUM0
F, I	Protein hfq	protein	71	18% helix, 42% strand	Q9HUM0
G	Protein hfq	protein	66	20% helix, 47% strand	Q9HUM0
J, K	Protein hfq	protein	68	19% helix, 44% strand	Q9HUM0

Ligands and binding sites

ZN · Zinc ion · metal · 14 copies · chains A, B, C, D, E, F, G, H, I, J, K, L

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	799	0.81	0.84	84	empty
2	779	0.78	0.82	64	empty
3	292	0.71	0.85	35	empty
4	206	0.56	0.79	47	empty
5	188	0.55	0.79	43	empty

Interfaces

22 interfaces between chains.

K–L · 871 Å² buried · 13 hydrogen bonds · protein-protein
A–B · 844 Å² buried · 13 hydrogen bonds · protein-protein
D–E · 841 Å² buried · 13 hydrogen bonds · protein-protein
B–C · 838 Å² buried · 12 hydrogen bonds · protein-protein
E–F · 819 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

3M4G · H57A HFQ from Pseudomonas Aeruginosa · the same entry in another collection · chain L against L, 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 Q9HUM0
Elsewhere: RCSB PDB 3M4G · PDBe 3M4G · UniProt Q9HUM0

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