3RN6
Crystal structure of Cytosine Deaminase from Escherichia Coli complexed with zinc and isoguanine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004131 | molecular_function | cytosine deaminase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006209 | biological_process | cytosine catabolic process |
| A | 0008198 | molecular_function | ferrous iron binding |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| A | 0016814 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines |
| A | 0019239 | molecular_function | deaminase activity |
| A | 0019858 | biological_process | cytosine metabolic process |
| A | 0035888 | molecular_function | isoguanine deaminase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PXN A 427 |
| Chain | Residue |
| A | GLN102 |
| A | TRP105 |
| A | LYS109 |
| A | GLU417 |
| A | GLU420 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 428 |
| Chain | Residue |
| A | ASP313 |
| A | HOH431 |
| A | HIS61 |
| A | HIS63 |
| A | HIS214 |
| A | HIS246 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 429 |
| Chain | Residue |
| A | HIS97 |
| A | HIS97 |
| A | GLU138 |
| A | GLU138 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE IGA A 430 |
| Chain | Residue |
| A | HIS63 |
| A | LEU81 |
| A | GLN156 |
| A | GLU217 |
| A | ASP313 |
| A | ASP314 |
| A | TRP319 |
| A | HOH431 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:11812140, ECO:0000305|PubMed:21545144, ECO:0000305|PubMed:21604715 |
| Chain | Residue | Details |
| A | GLU217 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715, ECO:0000269|Ref.14 |
| Chain | Residue | Details |
| A | HIS61 | |
| A | HIS63 | |
| A | HIS214 | |
| A | ASP313 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11812140, ECO:0000269|PubMed:15381761, ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715 |
| Chain | Residue | Details |
| A | GLN156 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11812140, ECO:0000269|PubMed:15381761, ECO:0000269|PubMed:21545144 |
| Chain | Residue | Details |
| A | TRP319 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | SITE: Activates the nucleophilic water => ECO:0000305|PubMed:21545144, ECO:0000305|PubMed:21604715 |
| Chain | Residue | Details |
| A | HIS246 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 710 |
| Chain | Residue | Details |
| A | HIS61 | metal ligand |
| A | HIS63 | metal ligand |
| A | GLN156 | electrostatic stabiliser |
| A | HIS214 | metal ligand |
| A | GLU217 | proton acceptor, proton donor |
| A | ASP313 | metal ligand |
