2EG5
The structure of xanthosine methyltransferase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008168 | molecular_function | methyltransferase activity |
A | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
A | 0009820 | biological_process | alkaloid metabolic process |
A | 0032259 | biological_process | methylation |
A | 0046872 | molecular_function | metal ion binding |
C | 0008168 | molecular_function | methyltransferase activity |
C | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
C | 0009820 | biological_process | alkaloid metabolic process |
C | 0032259 | biological_process | methylation |
C | 0046872 | molecular_function | metal ion binding |
E | 0008168 | molecular_function | methyltransferase activity |
E | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
E | 0009820 | biological_process | alkaloid metabolic process |
E | 0032259 | biological_process | methylation |
E | 0046872 | molecular_function | metal ion binding |
G | 0008168 | molecular_function | methyltransferase activity |
G | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
G | 0009820 | biological_process | alkaloid metabolic process |
G | 0032259 | biological_process | methylation |
G | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE SAH A 501 |
Chain | Residue |
A | TYR18 |
A | TYR142 |
A | CYS157 |
A | TYR158 |
A | CYS159 |
A | HOH522 |
A | HOH524 |
A | HOH577 |
A | HOH644 |
A | GLY61 |
A | ALA63 |
A | ASN100 |
A | ASP101 |
A | LEU102 |
A | GLY139 |
A | SER140 |
A | PHE141 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE XTS A 502 |
Chain | Residue |
A | ASN21 |
A | SER22 |
A | TYR24 |
A | ASN25 |
A | TYR158 |
A | GLN161 |
A | TRP162 |
A | SER316 |
A | TYR321 |
A | TYR356 |
site_id | AC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE SAH C 1501 |
Chain | Residue |
C | TYR18 |
C | GLY61 |
C | ALA63 |
C | ASN100 |
C | ASP101 |
C | LEU102 |
C | GLY139 |
C | SER140 |
C | PHE141 |
C | CYS157 |
C | TYR158 |
C | CYS159 |
C | HOH1503 |
C | HOH1508 |
C | HOH1558 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE XTS C 1502 |
Chain | Residue |
C | ASN21 |
C | SER22 |
C | TYR24 |
C | ASN25 |
C | TYR158 |
C | GLN161 |
C | TRP162 |
C | SER316 |
C | TYR321 |
C | TYR356 |
site_id | AC5 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE SAH E 2501 |
Chain | Residue |
E | TYR18 |
E | LEU29 |
E | GLY61 |
E | ALA63 |
E | ASN100 |
E | ASP101 |
E | GLY139 |
E | SER140 |
E | PHE141 |
E | TYR142 |
E | CYS157 |
E | TYR158 |
E | CYS159 |
E | TRP162 |
E | HOH2540 |
E | HOH2562 |
site_id | AC6 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE XTS E 2502 |
Chain | Residue |
E | ASN21 |
E | SER22 |
E | TYR24 |
E | ASN25 |
E | TYR158 |
E | GLN161 |
E | TRP162 |
E | SER316 |
E | TYR321 |
E | TYR356 |
E | HOH2550 |
E | HOH2564 |
E | HOH2598 |
site_id | AC7 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE SAH G 3501 |
Chain | Residue |
G | TYR18 |
G | GLY61 |
G | ALA63 |
G | ASN100 |
G | ASP101 |
G | LEU102 |
G | GLY139 |
G | SER140 |
G | PHE141 |
G | TYR142 |
G | CYS157 |
G | TYR158 |
G | CYS159 |
G | HOH3505 |
G | HOH3511 |
G | HOH3573 |
site_id | AC8 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE XTS G 3502 |
Chain | Residue |
G | TYR24 |
G | ASN25 |
G | TYR158 |
G | GLN161 |
G | TRP162 |
G | SER316 |
G | VAL320 |
G | TYR321 |
G | TYR356 |
G | ASN21 |
G | SER22 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:A4GE70 |
Chain | Residue | Details |
A | TYR18 | |
A | ASN67 | |
C | TYR18 | |
C | ASN67 | |
E | TYR18 | |
E | ASN67 | |
G | TYR18 | |
G | ASN67 |
site_id | SWS_FT_FI2 |
Number of Residues | 36 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17434991, ECO:0007744|PDB:2EG5 |
Chain | Residue | Details |
A | ASN21 | |
C | ASN21 | |
C | GLY61 | |
C | LEU99 | |
C | SER140 | |
C | CYS157 | |
C | TYR158 | |
C | SER316 | |
C | TYR321 | |
C | TYR356 | |
E | ASN21 | |
A | GLY61 | |
E | GLY61 | |
E | LEU99 | |
E | SER140 | |
E | CYS157 | |
E | TYR158 | |
E | SER316 | |
E | TYR321 | |
E | TYR356 | |
G | ASN21 | |
G | GLY61 | |
A | LEU99 | |
G | LEU99 | |
G | SER140 | |
G | CYS157 | |
G | TYR158 | |
G | SER316 | |
G | TYR321 | |
G | TYR356 | |
A | SER140 | |
A | CYS157 | |
A | TYR158 | |
A | SER316 | |
A | TYR321 | |
A | TYR356 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:A0A6C0WW36 |
Chain | Residue | Details |
A | CYS62 | |
C | CYS62 | |
E | CYS62 | |
G | CYS62 |
site_id | SWS_FT_FI4 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9FLN8 |
Chain | Residue | Details |
A | ASN179 | |
E | ASP261 | |
E | PHE263 | |
E | ASN264 | |
G | ASN179 | |
G | ASP261 | |
G | PHE263 | |
G | ASN264 | |
A | ASP261 | |
A | PHE263 | |
A | ASN264 | |
C | ASN179 | |
C | ASP261 | |
C | PHE263 | |
C | ASN264 | |
E | ASN179 |
site_id | SWS_FT_FI5 |
Number of Residues | 12 |
Details | SITE: Involved in substrate discrimination => ECO:0000250|UniProtKB:Q9FZN8 |
Chain | Residue | Details |
A | HIS155 | |
G | HIS155 | |
G | VAL267 | |
G | GLU331 | |
A | VAL267 | |
A | GLU331 | |
C | HIS155 | |
C | VAL267 | |
C | GLU331 | |
E | HIS155 | |
E | VAL267 | |
E | GLU331 |