2OGY
Asn199Ala Mutant of the 5-methyltetrahydrofolate corrinoid/iron sulfur protein methyltransferase complexed with methyltetrahydrofolate to 2.3 Angstrom resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005515 | molecular_function | protein binding |
A | 0005829 | cellular_component | cytosol |
A | 0008168 | molecular_function | methyltransferase activity |
A | 0008705 | molecular_function | methionine synthase activity |
A | 0009086 | biological_process | methionine biosynthetic process |
A | 0015977 | biological_process | carbon fixation |
A | 0031419 | molecular_function | cobalamin binding |
A | 0032259 | biological_process | methylation |
A | 0042558 | biological_process | pteridine-containing compound metabolic process |
A | 0044237 | biological_process | cellular metabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0102036 | molecular_function | methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase activity |
B | 0005509 | molecular_function | calcium ion binding |
B | 0005515 | molecular_function | protein binding |
B | 0005829 | cellular_component | cytosol |
B | 0008168 | molecular_function | methyltransferase activity |
B | 0008705 | molecular_function | methionine synthase activity |
B | 0009086 | biological_process | methionine biosynthetic process |
B | 0015977 | biological_process | carbon fixation |
B | 0031419 | molecular_function | cobalamin binding |
B | 0032259 | biological_process | methylation |
B | 0042558 | biological_process | pteridine-containing compound metabolic process |
B | 0044237 | biological_process | cellular metabolic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0102036 | molecular_function | methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA A 3001 |
Chain | Residue |
A | GLY222 |
A | ASP224 |
A | HOH3027 |
A | HOH3032 |
A | HOH3092 |
A | HOH3111 |
A | HOH3127 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA B 4001 |
Chain | Residue |
B | HOH4048 |
B | HOH4050 |
B | HOH4062 |
B | HOH4104 |
B | HOH4151 |
B | GLY222 |
B | ASP224 |
site_id | AC3 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE C2F A 3000 |
Chain | Residue |
A | GLU6 |
A | MET11 |
A | PHE12 |
A | ASP75 |
A | ASN96 |
A | ILE120 |
A | ASP160 |
A | GLY196 |
A | SER198 |
A | GLN202 |
A | ARG207 |
A | ILE227 |
A | HOH3002 |
A | HOH3003 |
A | HOH3008 |
A | HOH3058 |
A | HOH3098 |
A | HOH3123 |
site_id | AC4 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE C2F B 4000 |
Chain | Residue |
B | MET11 |
B | PHE12 |
B | ASP75 |
B | ASN96 |
B | ILE120 |
B | LEU122 |
B | ASP160 |
B | GLY196 |
B | SER198 |
B | GLN202 |
B | ARG207 |
B | HOH4002 |
B | HOH4003 |
B | HOH4004 |
B | HOH4006 |
B | HOH4049 |
B | HOH4122 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17172470, ECO:0000269|PubMed:22419154, ECO:0007744|PDB:4DJE, ECO:0007744|PDB:4DJF |
Chain | Residue | Details |
A | ASN96 | |
A | ASP160 | |
A | ALA199 | |
A | ARG207 | |
B | ASN96 | |
B | ASP160 | |
B | ALA199 | |
B | ARG207 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17172470, ECO:0000269|PubMed:22419154 |
Chain | Residue | Details |
A | LYS184 | |
A | GLY222 | |
A | ASP224 | |
B | LYS184 | |
B | GLY222 | |
B | ASP224 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17172470, ECO:0000269|PubMed:22419154, ECO:0007744|PDB:4DJF |
Chain | Residue | Details |
A | GLN202 | |
B | GLN202 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
A | ALA199 | |
B | ALA199 |