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Crystal structure of klebsiella pneumoniae protein orfy, pfam DUF336

Analyse Crystal structure of klebsiella pneumoniae protein orfy, pfam DUF336 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2A2L
Type: protein
Length: 576 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Unknown
UniProt: Q48422
Pockets: 5 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Unknown	protein	145	41% helix, 22% strand	Q48422
C, D	Unknown	protein	143	38% helix, 23% strand	Q48422

Pockets

5 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	1050	0.76	0.79	99	empty
2	128	0.64	0.88	25	empty
3	82	0.48	0.82	21	empty
4	66	0.46	0.83	20	empty
5	72	0.39	0.79	16	empty

Interfaces

5 interfaces between chains.

A–D · 1142 Å² buried · 27 hydrogen bonds · protein-protein
B–C · 1109 Å² buried · 22 hydrogen bonds · protein-protein
C–D · 801 Å² buried · 3 hydrogen bonds · protein-protein
A–B · 795 Å² buried · 6 hydrogen bonds · protein-protein
B–D · 692 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

2A2L · Crystal structure of Klebsiella pneumoniae protein ORFY, Pfam DUF336 · 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 Q48422
Elsewhere: RCSB PDB 2A2L · PDBe 2A2L · UniProt Q48422

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