MolNFT v1 · #99725 · protein

HIV protease in complex with SA526P

4MC1: “HIV protease in complex with SA526P”. X-ray diffraction, 2 ligands (526, CL), 1 pocket (best druggability 0.75). MolNFT v1 #99725 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4MC1
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protease
EC: 3.4.23.16
UniProt: P0C6F2
Ligands: 526, CL
Pockets: 1 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protease (EC 3.4.23.16)	protein	99	4% helix, 56% strand	P0C6F2

Ligands and binding sites

526 · (3S)-tetrahydrofuran-3-yl {(2S,3R)-4-[(4S)-4-tert-butyl-7-fluoro-1,1-dioxido-4,5-dihydro-1,2-benzothiazepin-2(3H)-yl]-3-hydroxy-1-phenylbutan-2-yl}carbamate · ligand · 2 copies · chains A, B
CL · Chloride ion · ion · 3 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	347	0.75	0.86	34	526

Interfaces

1 interface between chains.

A–B · 1858 Å² buried · 39 hydrogen bonds · protein-protein

Compared structures

4MC1 · HIV protease in complex with SA526P · 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 P0C6F2
Elsewhere: RCSB PDB 4MC1 · PDBe 4MC1 · UniProt P0C6F2

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