MolNFT v1 · #157187 · protein

Rbcs-like subdomain of ccmm

6MR1 · Carbon dioxide concentrating mechanism protein: “Rbcs-like subdomain of ccmm”. X-ray diffraction, 4 ligands (CO, SO4, SCN). MolNFT v1 #157187 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6MR1
Type: protein
Length: 174 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carbon dioxide concentrating mechanism protein
UniProt: Q8DKB5
Ligands: CO, SO4, SCN, CL

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carbon dioxide concentrating mechanism protein	protein	88	33% helix, 38% strand	Q8DKB5
B	Carbon dioxide concentrating mechanism protein	protein	86	33% helix, 38% strand	Q8DKB5

Ligands and binding sites

CO · Cobalt (II) ion · metal · 3 copies · chains A, B
SO4 · Sulfate ion · ion · 2 copies
SCN · Thiocyanate ion · ion · 2 copies · chains B
CL · Chloride ion · ion · chains A

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

Compared structures

6MR1 · RbcS-like subdomain of CcmM · the same entry in another collection · chain A against A, TM-score 1.00
Q8DKB5 · AlphaFold monomer V2.0 prediction for carboxysome assembly protein ccmm (Q8DKB5) · a predicted model of the same protein · chain B against A, TM-score 0.94

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 Q8DKB5
Elsewhere: RCSB PDB 6MR1 · PDBe 6MR1 · UniProt Q8DKB5

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