MolNFT v1 · #162916 · protein

DPP1 in complex with inhibitor

6RN7: “DPP1 in complex with inhibitor”. X-ray diffraction, 3 ligands (K9W, NAG, CL). MolNFT v1 #162916 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6RN7
Type: protein
Length: 348 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P53634
Ligands: K9W, NAG, CL

Structure

x-ray diffraction · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	118	—	P53634
B	—	protein	162	—	P53634
C	—	protein	68	—	P53634

Ligands and binding sites

K9W · (2~{S})-~{N}-[(2~{S})-1-azanyl-3-[4-(4-cyanophenyl) phenyl]propan-2-yl]pyrrolidine-2-carboxamide · ligand · chains A, B, C
NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, C, B
CL · Chloride ion · ion · chains B, C
DMS · Dimethyl sulfoxide · additive · 2 copies · chains A, B, C
GOL · Glycerol · additive · chains A, B

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

Compared structures

6RN7 · DPP1 in complex with inhibitor · the same entry in another collection · chain A against A, TM-score 1.00
P53634 · AlphaFold monomer V2.0 prediction for dipeptidyl peptidase 1 (P53634) · a predicted model of the same protein · chain B 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 P53634
Elsewhere: RCSB PDB 6RN7 · PDBe 6RN7 · UniProt P53634

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