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Crystal structure of a putative structural protein from klebsiella pneumoniae

Analyse Crystal structure of a putative structural protein from klebsiella pneumoniae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7TMV
Type: protein
Length: 314 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative structural protein
UniProt: A0A0H3GMY9
Ligands: ZN
Pockets: 4 · best druggability 0.55

Structure

x-ray diffraction · 2 distinct chains · 83% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative structural protein	protein	159	82% helix, 0% strand	A0A0H3GMY9
B	Putative structural protein	protein	155	85% helix, 0% strand	A0A0H3GMY9

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	115	0.55	0.83	21	empty
2	67	0.54	0.87	16	empty
3	133	0.42	0.75	28	empty
4	63	0.37	0.79	21	empty

Interfaces

1 interface between chains.

A–B · 1327 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

7TMV · Crystal structure of a Putative structural protein from Klebsiella pneumoniae · 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
Every structure of UniProt A0A0H3GMY9
Elsewhere: RCSB PDB 7TMV · PDBe 7TMV · UniProt A0A0H3GMY9

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