MolNFT v1 · #143105 · protein

Crystal structure of adenosylhomocysteinase from elizabethkingia anophelis NUHP1 in complex with NAD and adenosine

6APH: “Crystal structure of adenosylhomocysteinase from elizabethkingia anophelis NUHP1 in complex with NAD and…”. X-ray diffraction, 2 ligands (NAD, ADN), 5 pockets (best druggability 0.70). MolNFT v1 #143105 on GenesisL1: 3D structure…

PDB: 6APH
Type: protein
Length: 432 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Adenosylhomocysteinase
EC: 3.3.1.1
UniProt: A0A077EDS4
Ligands: NAD, ADN
Pockets: 5 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Adenosylhomocysteinase (EC 3.3.1.1)	protein	432	49% helix, 16% strand	A0A077EDS4

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
ADN · Adenosine · ligand · chains A
MPD · (4S)-2-methyl-2,4-pentanediol · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	358	0.70	0.83	55	NAD, ADN
2	114	0.40	0.75	15	empty
3	68	0.32	0.75	14	empty
4	62	0.30	0.75	19	empty
5	58	0.28	0.74	14	empty

Compared structures

6APH · Crystal structure of Adenosylhomocysteinase from Elizabethkingia anophelis NUHP1 in… · 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 A0A077EDS4
Elsewhere: RCSB PDB 6APH · PDBe 6APH · UniProt A0A077EDS4

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