MolNFT v1 · #98872 · protein

Crystal structure of NHERF1 PDZ1 domain complexed with the CXCR2 C- terminal tail in P21 space group

4LMM · NA(+)/H(+) exchange regulatory cofactor nhe-RF1: “Crystal structure of NHERF1 PDZ1 domain complexed with the CXCR2 C- terminal tail in P21 space group”. X-ray diffraction, 1 ligand (CL), 1 pocket (best druggability 0.33). MolNFT v1…

PDB: 4LMM
Type: protein
Length: 91 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: NA(+)/H(+) exchange regulatory cofactor nhe-RF1
UniProt: O14745
Ligands: CL
Pockets: 1 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NA(+)/H(+) exchange regulatory cofactor nhe-RF1	protein	91	15% helix, 31% strand	O14745

Ligands and binding sites

CL · Chloride ion · ion · chains A
ACY · Acetic acid · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	61	0.33	0.76	11	empty

Compared structures

4LMM · Crystal structure of NHERF1 PDZ1 domain complexed with the CXCR2 C-terminal tail in P21… · the same entry in another collection · chain A against A, TM-score 1.00
O14745 · AlphaFold monomer V2.0 prediction for NA(+)/H(+) exchange regulatory cofactor nhe-RF1… · a predicted model of the same protein · chain A against A, TM-score 0.90

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 O14745
Elsewhere: RCSB PDB 4LMM · PDBe 4LMM · UniProt O14745

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.