1O5Q
Crystal Structure of Pyruvate and Mg2+ bound 2-methylisocitrate lyase (PrpB) from Salmonella typhimurium
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016833 | molecular_function | oxo-acid-lyase activity |
| A | 0019629 | biological_process | propionate catabolic process, 2-methylcitrate cycle |
| A | 0046421 | molecular_function | methylisocitrate lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0140677 | molecular_function | molecular function activator activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016833 | molecular_function | oxo-acid-lyase activity |
| B | 0019629 | biological_process | propionate catabolic process, 2-methylcitrate cycle |
| B | 0046421 | molecular_function | methylisocitrate lyase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0140677 | molecular_function | molecular function activator activity |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016833 | molecular_function | oxo-acid-lyase activity |
| C | 0019629 | biological_process | propionate catabolic process, 2-methylcitrate cycle |
| C | 0046421 | molecular_function | methylisocitrate lyase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0140677 | molecular_function | molecular function activator activity |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016833 | molecular_function | oxo-acid-lyase activity |
| D | 0019629 | biological_process | propionate catabolic process, 2-methylcitrate cycle |
| D | 0046421 | molecular_function | methylisocitrate lyase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0140677 | molecular_function | molecular function activator activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 1301 |
| Chain | Residue |
| A | ASP85 |
| A | PYR1302 |
| A | HOH1452 |
| A | HOH1455 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 2301 |
| Chain | Residue |
| B | HOH2456 |
| B | ASP85 |
| B | ARG158 |
| B | PYR2302 |
| B | HOH2400 |
| B | HOH2454 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 3301 |
| Chain | Residue |
| C | ASP85 |
| C | PYR3302 |
| C | HOH3379 |
| C | HOH3403 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 4301 |
| Chain | Residue |
| D | ASP85 |
| D | PYR4302 |
| D | HOH4376 |
| D | HOH4377 |
| D | HOH4380 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PYR A 1302 |
| Chain | Residue |
| A | TYR43 |
| A | SER45 |
| A | GLY46 |
| A | GLY47 |
| A | ASP85 |
| A | ARG158 |
| A | PRO236 |
| A | MG1301 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PYR B 2302 |
| Chain | Residue |
| B | TYR43 |
| B | SER45 |
| B | GLY46 |
| B | GLY47 |
| B | ASP85 |
| B | ARG158 |
| B | PRO236 |
| B | MG2301 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PYR C 3302 |
| Chain | Residue |
| C | TYR43 |
| C | SER45 |
| C | GLY46 |
| C | GLY47 |
| C | ASP85 |
| C | ARG158 |
| C | PRO236 |
| C | MG3301 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PYR D 4302 |
| Chain | Residue |
| D | TYR43 |
| D | SER45 |
| D | GLY47 |
| D | ASP85 |
| D | ARG158 |
| D | PRO236 |
| D | MG4301 |
| D | HOH4385 |
Functional Information from PROSITE/UniProt
| site_id | PS00161 |
| Number of Residues | 6 |
| Details | ISOCITRATE_LYASE Isocitrate lyase signature. KRCGHR |
| Chain | Residue | Details |
| A | LYS121-ARG126 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14575713 |
| Chain | Residue | Details |
| A | GLY46 | |
| D | GLY46 | |
| D | ALA86 | |
| D | THR159 | |
| A | ALA86 | |
| A | THR159 | |
| B | GLY46 | |
| B | ALA86 | |
| B | THR159 | |
| C | GLY46 | |
| C | ALA86 | |
| C | THR159 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01939 |
| Chain | Residue | Details |
| A | ILE88 | |
| B | ILE211 | |
| B | ALA242 | |
| B | ASN271 | |
| C | ILE88 | |
| C | GLY124 | |
| C | ALA189 | |
| C | ILE211 | |
| C | ALA242 | |
| C | ASN271 | |
| D | ILE88 | |
| A | GLY124 | |
| D | GLY124 | |
| D | ALA189 | |
| D | ILE211 | |
| D | ALA242 | |
| D | ASN271 | |
| A | ALA189 | |
| A | ILE211 | |
| A | ALA242 | |
| A | ASN271 | |
| B | ILE88 | |
| B | GLY124 | |
| B | ALA189 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1f8m |
| Chain | Residue | Details |
| A | HIS113 | |
| A | ARG158 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1f8m |
| Chain | Residue | Details |
| B | HIS113 | |
| B | ARG158 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1f8m |
| Chain | Residue | Details |
| C | HIS113 | |
| C | ARG158 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1f8m |
| Chain | Residue | Details |
| D | HIS113 | |
| D | ARG158 |
