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Ocpa complexed cprk (C200S)

Analyse Ocpa complexed cprk (C200S) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3E6B
Type: protein
Length: 416 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cyclic nucleotide-binding protein
UniProt: Q18R04
Ligands: 3C4
Pockets: 5 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cyclic nucleotide-binding protein	protein	208	41% helix, 29% strand	Q18R04
B	Cyclic nucleotide-binding protein	protein	208	40% helix, 27% strand	Q18R04

Ligands and binding sites

3C4 · (3-chloro-4-hydroxyphenyl)acetic acid · ligand · 2 copies · chains A, B

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

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	64	0.74	0.98	16	3C4
2	67	0.72	0.97	16	3C4
3	177	0.49	0.77	26	empty
4	75	0.35	0.76	21	empty
5	56	0.35	0.78	14	empty

Interfaces

1 interface between chains.

A–B · 2904 Å² buried · 30 hydrogen bonds · protein-protein

Compared structures

3E6B · OCPA complexed CprK (C200S) · 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 Q18R04
Elsewhere: RCSB PDB 3E6B · PDBe 3E6B · UniProt Q18R04

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