Co-bound nitrogenase mofe-protein from a. vinelandii

Structure

x-ray diffraction · 2 distinct chains · 50% helix, 13% strand (DSSP).

Ligands and binding sites

• ICE · iron-sulfur-molybdenum cluster with interstitial carbon · ligand · 4 copies · chains A, B, C, D
• HCA · 3-hydroxy-3-carboxy-adipic acid · ligand · 2 copies · chains A, B, C, D
• CLF · FE(8)-S(7) cluster · ligand · 2 copies · chains A, B, C, D
• FE2 · Fe (II) ion · metal · 2 copies · chains B, C, D, A
• CMO · Carbon monoxide · ion · 6 copies · chains A, B, D, C
• IMD · Imidazole · additive · 8 copies · chains A, B, C, D

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

Pockets

20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

Interfaces

5 interfaces between chains.

• A–B · 4708 Ų buried · 59 hydrogen bonds · protein-protein
• C–D · 4676 Ų buried · 57 hydrogen bonds · protein-protein
• B–D · 3128 Ų buried · 61 hydrogen bonds · protein-protein
• B–C · 1371 Ų buried · 16 hydrogen bonds · protein-protein
• A–D · 1356 Ų buried · 14 hydrogen bonds · protein-protein

Compared structures

• 4TKV · CO-bound Nitrogenase MoFe-protein from A. vinelandii · the same entry in another collection · chain D against D, TM-score 1.00
• P07328 · AlphaFold monomer V2.0 prediction for nitrogenase molybdenum-iron protein alpha chain… · a predicted model of the same protein · chain A against A, TM-score 1.00
• P07329 · AlphaFold monomer V2.0 prediction for nitrogenase molybdenum-iron protein beta chain… · 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 P07328
• Every structure of UniProt P07329
• Elsewhere: RCSB PDB 4TKV · PDBe 4TKV · UniProt P07328 · UniProt P07329