4QQU
Crystal structure of the cobalamin-independent methionine synthase enzyme in a closed conformation
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003871 | molecular_function | 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005634 | cellular_component | nucleus |
| A | 0005829 | cellular_component | cytosol |
| A | 0006555 | biological_process | methionine metabolic process |
| A | 0006696 | biological_process | ergosterol biosynthetic process |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008172 | molecular_function | S-methyltransferase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0008705 | molecular_function | methionine synthase activity |
| A | 0009086 | biological_process | methionine biosynthetic process |
| A | 0009277 | cellular_component | fungal-type cell wall |
| A | 0009986 | cellular_component | cell surface |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019280 | biological_process | L-methionine biosynthetic process from homoserine via O-acetyl-L-homoserine and cystathionine |
| A | 0030446 | cellular_component | hyphal cell wall |
| A | 0032259 | biological_process | methylation |
| A | 0034605 | biological_process | cellular response to heat |
| A | 0044416 | biological_process | obsolete induction by symbiont of host defense response |
| A | 0046084 | biological_process | adenine biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0062040 | cellular_component | fungal biofilm matrix |
| A | 0071266 | biological_process | 'de novo' L-methionine biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HCS A 801 |
| Chain | Residue |
| A | ILE446 |
| A | CYS739 |
| A | GLY740 |
| A | ZN802 |
| A | 39S805 |
| A | GLY447 |
| A | SER448 |
| A | GLU499 |
| A | MET505 |
| A | MET566 |
| A | ASP614 |
| A | HIS657 |
| A | CYS659 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 802 |
| Chain | Residue |
| A | HIS657 |
| A | CYS659 |
| A | CYS739 |
| A | HCS801 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 803 |
| Chain | Residue |
| A | ARG99 |
| A | TYR527 |
| A | ARG530 |
| A | HIS707 |
| A | THR743 |
| A | ARG744 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 804 |
| Chain | Residue |
| A | PRO665 |
| A | ASN666 |
| A | LYS669 |
| A | GLU694 |
| A | TYR695 |
| A | PRO696 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE 39S A 805 |
| Chain | Residue |
| A | ARG16 |
| A | LYS19 |
| A | ASN126 |
| A | LYS330 |
| A | GLN451 |
| A | LYS453 |
| A | ARG456 |
| A | ARG459 |
| A | ASN503 |
| A | ASP504 |
| A | MET505 |
| A | TRP523 |
| A | SER526 |
| A | ARG530 |
| A | TYR531 |
| A | VAL532 |
| A | TRP576 |
| A | THR743 |
| A | HCS801 |
| A | HOH915 |
| A | HOH923 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:25545590 |
| Chain | Residue | Details |
| A | HIS707 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24524835, ECO:0000269|PubMed:25545590, ECO:0007744|PDB:4L64, ECO:0007744|PDB:4L65, ECO:0007744|PDB:4L6H, ECO:0007744|PDB:4QQU |
| Chain | Residue | Details |
| A | LYS19 | |
| A | TYR527 | |
| A | TRP576 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24524835, ECO:0000269|PubMed:25545590, ECO:0007744|PDB:4L65, ECO:0007744|PDB:4L6H, ECO:0007744|PDB:4QQU |
| Chain | Residue | Details |
| A | ASN126 | |
| A | ASP504 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24524835, ECO:0007744|PDB:4L61, ECO:0007744|PDB:4L65 |
| Chain | Residue | Details |
| A | ILE446 | |
| A | GLU499 | |
| A | ASP614 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24524835, ECO:0000269|PubMed:25545590, ECO:0007744|PDB:4L64, ECO:0007744|PDB:4L65, ECO:0007744|PDB:4QQU |
| Chain | Residue | Details |
| A | ARG530 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21689631, ECO:0000269|PubMed:24524835, ECO:0000269|PubMed:25545590, ECO:0007744|PDB:3PPC, ECO:0007744|PDB:3PPG, ECO:0007744|PDB:4L5Z, ECO:0007744|PDB:4L61, ECO:0007744|PDB:4L64, ECO:0007744|PDB:4L65, ECO:0007744|PDB:4L6H, ECO:0007744|PDB:4L6O, ECO:0007744|PDB:4QQU |
| Chain | Residue | Details |
| A | HIS657 | |
| A | CYS659 | |
| A | CYS739 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21689631, ECO:0000269|PubMed:24524835, ECO:0007744|PDB:3PPG, ECO:0007744|PDB:4L61, ECO:0007744|PDB:4L64, ECO:0007744|PDB:4L6O |
| Chain | Residue | Details |
| A | GLU679 |
