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Crystal structure of SEL1 repeat protein from oxalobacter formigenes

Analyse Crystal structure of SEL1 repeat protein from oxalobacter formigenes in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6ORK
Type: protein
Length: 737 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SEL1 repeat protein
EC: 3.5.2.6
UniProt: C3X9F9
Pockets: 6 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 71% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	SEL1 repeat protein (EC 3.5.2.6)	protein	246	71% helix, 0% strand	C3X9F9
B	SEL1 repeat protein (EC 3.5.2.6)	protein	245	72% helix, 0% strand	C3X9F9

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	776	0.79	0.83	105	empty
2	681	0.77	0.82	70	empty
3	143	0.61	0.85	32	empty
4	93	0.38	0.76	18	empty
5	83	0.36	0.76	19	empty

Interfaces

2 interfaces between chains.

A–B · 1182 Å² buried · 12 hydrogen bonds · protein-protein
B–C · 1065 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 27 modified (engineered).

Compared structures

6ORK · Crystal structure of Sel1 repeat protein from Oxalobacter formigenes · 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 C3X9F9
Elsewhere: RCSB PDB 6ORK · PDBe 6ORK · UniProt C3X9F9

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