MolNFT v1 · #12648 · protein

Structure of ahpd from mycobacterium tuberculosis, a novel enzyme with thioredoxin-like activity.

1KNC · Ahpd protein: “Structure of ahpd from mycobacterium tuberculosis, a novel enzyme with thioredoxin-like activity.”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.81). MolNFT v1 #12648 on GenesisL1: 3D structure…

PDB: 1KNC
Type: protein
Length: 521 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ahpd protein
UniProt: P0A5N4
Ligands: SO4
Pockets: 1 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 74% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Ahpd protein	protein	174	75% helix, 0% strand	P0A5N4
C	Ahpd protein	protein	173	74% helix, 0% strand	P0A5N4

Ligands and binding sites

SO4 · Sulfate ion · ion · 17 copies · chains A, C, 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	830	0.81	0.84	85	SO4

Interfaces

3 interfaces between chains.

A–B · 1496 Å² buried · 19 hydrogen bonds · protein-protein
A–C · 1486 Å² buried · 20 hydrogen bonds · protein-protein
B–C · 1481 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

1KNC · Structure of AhpD from Mycobacterium tuberculosis, a novel enzyme with thioredoxin-like… · 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 P0A5N4
Elsewhere: RCSB PDB 1KNC · PDBe 1KNC · UniProt P0A5N4

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