4IRQ
Crystal structure of catalytic domain of human beta1,4galactosyltransferase 7 in closed conformation in complex with manganese and UDP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0016757 | molecular_function | glycosyltransferase activity |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0016757 | molecular_function | glycosyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 401 |
| Chain | Residue |
| A | ASP165 |
| A | HIS257 |
| A | HIS259 |
| A | UDP402 |
| A | HOH501 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE UDP A 402 |
| Chain | Residue |
| A | PHE139 |
| A | ASP163 |
| A | VAL164 |
| A | ASP165 |
| A | TYR194 |
| A | TRP224 |
| A | HIS257 |
| A | HIS259 |
| A | ARG266 |
| A | MN401 |
| A | TRS403 |
| A | HOH501 |
| A | HOH531 |
| A | PRO100 |
| A | PHE101 |
| A | ARG102 |
| A | ARG104 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TRS A 403 |
| Chain | Residue |
| A | TYR199 |
| A | TRP224 |
| A | GLY225 |
| A | GLU227 |
| A | ASP228 |
| A | UDP402 |
| A | HOH514 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 401 |
| Chain | Residue |
| B | ASP165 |
| B | HIS257 |
| B | HIS259 |
| B | UDP402 |
| B | HOH501 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE UDP B 402 |
| Chain | Residue |
| B | PRO100 |
| B | PHE101 |
| B | ARG102 |
| B | ARG104 |
| B | PHE139 |
| B | ASP163 |
| B | VAL164 |
| B | ASP165 |
| B | TYR194 |
| B | TRP224 |
| B | HIS257 |
| B | HIS259 |
| B | ARG266 |
| B | MN401 |
| B | TRS403 |
| B | HOH501 |
| B | HOH505 |
| B | HOH524 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE TRS B 403 |
| Chain | Residue |
| B | TYR194 |
| B | TYR199 |
| B | TRP224 |
| B | GLY225 |
| B | GLU227 |
| B | ASP228 |
| B | UDP402 |
| B | HOH532 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN C 401 |
| Chain | Residue |
| C | ASP165 |
| C | HIS257 |
| C | HIS259 |
| C | UDP402 |
| C | HOH501 |
| site_id | AC8 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE UDP C 402 |
| Chain | Residue |
| C | PRO100 |
| C | PHE101 |
| C | ARG102 |
| C | ARG104 |
| C | PHE139 |
| C | ASP163 |
| C | VAL164 |
| C | ASP165 |
| C | TYR194 |
| C | TRP224 |
| C | HIS257 |
| C | HIS259 |
| C | ARG266 |
| C | MN401 |
| C | TRS403 |
| C | HOH517 |
| C | HOH563 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TRS C 403 |
| Chain | Residue |
| C | ARG141 |
| C | TYR199 |
| C | GLY225 |
| C | GLU227 |
| C | ASP228 |
| C | UDP402 |
| C | HOH526 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN D 401 |
| Chain | Residue |
| D | ASP165 |
| D | HIS257 |
| D | HIS259 |
| D | UDP402 |
| D | HOH501 |
| site_id | BC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE UDP D 402 |
| Chain | Residue |
| D | ASP163 |
| D | VAL164 |
| D | ASP165 |
| D | TYR194 |
| D | TRP224 |
| D | HIS257 |
| D | HIS259 |
| D | ARG266 |
| D | MN401 |
| D | TRS403 |
| D | HOH533 |
| D | HOH536 |
| D | HOH574 |
| D | PRO100 |
| D | PHE101 |
| D | ARG102 |
| D | ARG104 |
| D | PHE139 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE TRS D 403 |
| Chain | Residue |
| D | ARG141 |
| D | TYR194 |
| D | TYR199 |
| D | TRP224 |
| D | GLY225 |
| D | GLU227 |
| D | ASP228 |
| D | UDP402 |
| D | HOH544 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24052259","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4IRP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4IRQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24052259","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24052259","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4IRQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
