3OS4
The Crystal Structure of Nicotinate Phosphoribosyltransferase from Yersinia pestis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004516 | molecular_function | nicotinate phosphoribosyltransferase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0009435 | biological_process | NAD+ biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
| A | 0034355 | biological_process | NAD+ biosynthetic process via the salvage pathway |
| B | 0004516 | molecular_function | nicotinate phosphoribosyltransferase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0009435 | biological_process | NAD+ biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
| B | 0034355 | biological_process | NAD+ biosynthetic process via the salvage pathway |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 410 |
| Chain | Residue |
| A | ARG239 |
| A | ASP271 |
| A | HOH542 |
| A | HOH666 |
| A | HOH902 |
| A | HOH927 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 411 |
| Chain | Residue |
| A | HOH676 |
| A | HOH878 |
| B | HOH652 |
| A | VAL216 |
| A | GLY217 |
| A | FMT414 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PEG A 412 |
| Chain | Residue |
| A | GLN3 |
| A | SER6 |
| A | PRO7 |
| A | GLU300 |
| A | GLY303 |
| A | ASP305 |
| A | HOH514 |
| A | HOH573 |
| A | HOH680 |
| A | HOH729 |
| A | HOH731 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT A 414 |
| Chain | Residue |
| A | MSE172 |
| A | THR218 |
| A | ARG282 |
| A | GOL411 |
| A | HOH693 |
| A | HOH937 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACY A 415 |
| Chain | Residue |
| A | ASP83 |
| A | ILE289 |
| A | GLU290 |
| A | GLU293 |
| A | HOH697 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 417 |
| Chain | Residue |
| A | GLU45 |
| A | LEU47 |
| A | LEU107 |
| A | HOH686 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 418 |
| Chain | Residue |
| A | ALA37 |
| A | VAL118 |
| A | ILE119 |
| A | TRP121 |
| A | GLU122 |
| A | GLU222 |
| A | ILE357 |
| A | LYS358 |
| A | LEU359 |
| A | HOH796 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 419 |
| Chain | Residue |
| A | ARG182 |
| A | HIS186 |
| A | HOH747 |
| A | HOH808 |
| A | HOH918 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 420 |
| Chain | Residue |
| A | LYS153 |
| A | ASP318 |
| A | LEU319 |
| A | ILE339 |
| A | ARG342 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT A 421 |
| Chain | Residue |
| A | ARG92 |
| A | LYS94 |
| A | PEG422 |
| A | HOH692 |
| A | HOH801 |
| A | HOH860 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG A 422 |
| Chain | Residue |
| A | GLY62 |
| A | ARG92 |
| A | PHE93 |
| A | FMT421 |
| A | HOH746 |
| A | HOH859 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PEG B 410 |
| Chain | Residue |
| B | MSE172 |
| B | GLY217 |
| B | THR218 |
| B | ILE255 |
| B | ARG282 |
| B | HOH568 |
| B | HOH674 |
| B | HOH675 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 411 |
| Chain | Residue |
| A | GLN229 |
| A | PRO366 |
| A | GLN387 |
| B | ARG136 |
| B | HOH786 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 412 |
| Chain | Residue |
| A | GLN148 |
| A | HOH605 |
| A | HOH706 |
| B | GLN243 |
| B | PHE274 |
| B | ARG277 |
| B | HOH472 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 415 |
| Chain | Residue |
| B | LEU47 |
| B | LYS106 |
| B | LEU107 |
| B | HOH687 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT B 416 |
| Chain | Residue |
| A | ASP194 |
| B | GLU361 |
| B | ASP364 |
| site_id | BC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 417 |
| Chain | Residue |
| B | ILE119 |
| B | TRP121 |
| B | GLU122 |
| B | GLU222 |
| B | ILE357 |
| B | LYS358 |
| B | LEU359 |
| B | HOH795 |
| B | LYS19 |
| B | VAL118 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 418 |
| Chain | Residue |
| B | TYR30 |
| B | ARG31 |
| B | HIS32 |
| B | HOH797 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 419 |
| Chain | Residue |
| B | SER75 |
| B | HOH501 |
| B | HOH671 |
| B | HOH690 |
| B | HOH870 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphohistidine; by autocatalysis","evidences":[{"source":"HAMAP-Rule","id":"MF_00570","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
