Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006551 | biological_process | L-leucine metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006551 | biological_process | L-leucine metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SF4 A 301 |
| Chain | Residue |
| A | CYS125 |
| A | CYS164 |
| A | THR165 |
| B | CYS125 |
| B | CYS164 |
| B | THR165 |
| site_id | AC2 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE ADP A 302 |
| Chain | Residue |
| A | ALA12 |
| A | LYS14 |
| A | GLY101 |
| A | GLY102 |
| A | GLY130 |
| A | ASP134 |
| A | VAL144 |
| A | SER145 |
| A | GLY214 |
| A | GLY215 |
| A | VAL216 |
| A | ARG218 |
| A | GLN241 |
| A | MG303 |
| A | CL307 |
| A | HOH423 |
| A | HOH429 |
| A | HOH442 |
| A | HOH449 |
| A | HOH463 |
| A | HOH466 |
| A | HOH476 |
| A | HOH505 |
| A | HOH509 |
| A | HOH522 |
| A | GLY9 |
| A | SER10 |
| A | THR11 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 303 |
| Chain | Residue |
| A | ADP302 |
| A | HOH462 |
| A | HOH463 |
| A | HOH465 |
| A | HOH521 |
| A | HOH522 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT A 304 |
| Chain | Residue |
| A | SER151 |
| A | ARG224 |
| A | HOH433 |
| A | HOH479 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT A 305 |
| Chain | Residue |
| A | SER81 |
| A | GLY114 |
| A | ARG115 |
| A | LEU116 |
| A | HOH483 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 306 |
| Chain | Residue |
| A | ILE239 |
| A | PRO240 |
| A | GLN241 |
| A | HOH428 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 307 |
| Chain | Residue |
| A | ALA12 |
| A | SER31 |
| A | GLN241 |
| A | ADP302 |
| site_id | AC8 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE ADP B 301 |
| Chain | Residue |
| B | GLY9 |
| B | SER10 |
| B | THR11 |
| B | ALA12 |
| B | LYS14 |
| B | GLY101 |
| B | GLY102 |
| B | GLY130 |
| B | ASP134 |
| B | SER145 |
| B | GLY214 |
| B | GLY215 |
| B | VAL216 |
| B | ARG218 |
| B | GLN241 |
| B | MG302 |
| B | NH4304 |
| B | HOH414 |
| B | HOH430 |
| B | HOH431 |
| B | HOH432 |
| B | HOH440 |
| B | HOH441 |
| B | HOH442 |
| B | HOH475 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 302 |
| Chain | Residue |
| B | ADP301 |
| B | HOH429 |
| B | HOH430 |
| B | HOH473 |
| B | HOH474 |
| B | HOH475 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT B 303 |
| Chain | Residue |
| B | ILE239 |
| B | PRO240 |
| B | GLN241 |
| B | LEU242 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NH4 B 304 |
| Chain | Residue |
| B | ALA12 |
| B | SER31 |
| B | GLN241 |
| B | ADP301 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22827463","evidenceCode":"ECO:0000269"}]} |
