3F9T
Crystal structure of L-tyrosine decarboxylase MfnA (EC 4.1.1.25) (NP_247014.1) from METHANOCOCCUS JANNASCHII at 2.11 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004068 | molecular_function | aspartate 1-decarboxylase activity |
| A | 0004837 | molecular_function | tyrosine decarboxylase activity |
| A | 0015937 | biological_process | coenzyme A biosynthetic process |
| A | 0016830 | molecular_function | carbon-carbon lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 2001120 | biological_process | methanofuran biosynthetic process |
| B | 0004068 | molecular_function | aspartate 1-decarboxylase activity |
| B | 0004837 | molecular_function | tyrosine decarboxylase activity |
| B | 0015937 | biological_process | coenzyme A biosynthetic process |
| B | 0016830 | molecular_function | carbon-carbon lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 2001120 | biological_process | methanofuran biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP A 500 |
| Chain | Residue |
| A | MSE37 |
| A | ASP242 |
| A | HIS244 |
| A | LYS245 |
| A | HOH580 |
| A | HOH587 |
| A | HOH700 |
| B | THR285 |
| A | GLY93 |
| A | GLY94 |
| A | THR95 |
| A | ASN98 |
| A | HIS132 |
| A | THR181 |
| A | ASP206 |
| A | ALA208 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP B 500 |
| Chain | Residue |
| A | THR285 |
| B | MSE37 |
| B | GLY93 |
| B | GLY94 |
| B | THR95 |
| B | ASN98 |
| B | HIS132 |
| B | THR181 |
| B | ASP206 |
| B | ALA208 |
| B | ASP242 |
| B | HIS244 |
| B | LYS245 |
| B | HOH482 |
| B | HOH506 |
| B | HOH719 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MPD B 397 |
| Chain | Residue |
| A | PRO272 |
| A | HOH512 |
| B | ALA131 |
| B | HIS132 |
| B | HOH519 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 397 |
| Chain | Residue |
| A | ILE129 |
| A | ALA131 |
| A | HOH539 |
| B | HOH714 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MPD A 398 |
| Chain | Residue |
| A | ASP50 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_01610, ECO:0000269|Ref.4 |
| Chain | Residue | Details |
| A | LYS245 | |
| B | LYS245 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bjo |
| Chain | Residue | Details |
| A | LYS229 | |
| A | PHE133 | |
| A | ASP206 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bjo |
| Chain | Residue | Details |
| B | LYS229 | |
| B | PHE133 | |
| B | ASP206 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bjo |
| Chain | Residue | Details |
| A | LYS245 | |
| A | PHE135 | |
| A | ASP206 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bjo |
| Chain | Residue | Details |
| B | LYS245 | |
| B | PHE135 | |
| B | ASP206 |
