MolNFT v1 · #189314 · protein

Crystal structure of the lanthipeptide zinc-metallopeptidase eryp mutant E802R from saccharopolyspora erythraea

7V9O · Alanine aminopeptidase: “Crystal structure of the lanthipeptide zinc-metallopeptidase eryp mutant E802R from saccharopolyspora…”. X-ray diffraction, 1 ligand (ZN), 5 pockets (best druggability 0.77). MolNFT v1 #189314 on GenesisL1…

PDB: 7V9O
Type: protein
Length: 860 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alanine aminopeptidase
EC: 3.4.11.2
UniProt: A4F9D7
Ligands: ZN
Pockets: 5 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alanine aminopeptidase (EC 3.4.11.2)	protein	860	45% helix, 22% strand	A4F9D7

Ligands and binding sites

ZN · Zinc ion · metal · chains A
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A

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

Pockets

5 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	735	0.77	0.81	79	ZN
2	524	0.74	0.82	59	empty
3	190	0.59	0.82	30	MES
4	98	0.39	0.76	21	empty
5	75	0.31	0.73	11	empty

Compared structures

7V9O · Crystal structure of the lanthipeptide zinc-metallopeptidase EryP mutant E802R from… · 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 A4F9D7
Elsewhere: RCSB PDB 7V9O · PDBe 7V9O · UniProt A4F9D7

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