4QPZ
Crystal structure of the formolase FLS_v2 in space group P 21
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003984 | molecular_function | acetolactate synthase activity |
| A | 0005948 | cellular_component | acetolactate synthase complex |
| A | 0009097 | biological_process | isoleucine biosynthetic process |
| A | 0009099 | biological_process | L-valine biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0030976 | molecular_function | thiamine pyrophosphate binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003984 | molecular_function | acetolactate synthase activity |
| B | 0005948 | cellular_component | acetolactate synthase complex |
| B | 0009097 | biological_process | isoleucine biosynthetic process |
| B | 0009099 | biological_process | L-valine biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0030976 | molecular_function | thiamine pyrophosphate binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0003984 | molecular_function | acetolactate synthase activity |
| C | 0005948 | cellular_component | acetolactate synthase complex |
| C | 0009097 | biological_process | isoleucine biosynthetic process |
| C | 0009099 | biological_process | L-valine biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0019752 | biological_process | carboxylic acid metabolic process |
| C | 0030976 | molecular_function | thiamine pyrophosphate binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0003984 | molecular_function | acetolactate synthase activity |
| D | 0005948 | cellular_component | acetolactate synthase complex |
| D | 0009097 | biological_process | isoleucine biosynthetic process |
| D | 0009099 | biological_process | L-valine biosynthetic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0019752 | biological_process | carboxylic acid metabolic process |
| D | 0030976 | molecular_function | thiamine pyrophosphate binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| E | 0000287 | molecular_function | magnesium ion binding |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0003984 | molecular_function | acetolactate synthase activity |
| E | 0005948 | cellular_component | acetolactate synthase complex |
| E | 0009097 | biological_process | isoleucine biosynthetic process |
| E | 0009099 | biological_process | L-valine biosynthetic process |
| E | 0016829 | molecular_function | lyase activity |
| E | 0019752 | biological_process | carboxylic acid metabolic process |
| E | 0030976 | molecular_function | thiamine pyrophosphate binding |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| F | 0000287 | molecular_function | magnesium ion binding |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0003984 | molecular_function | acetolactate synthase activity |
| F | 0005948 | cellular_component | acetolactate synthase complex |
| F | 0009097 | biological_process | isoleucine biosynthetic process |
| F | 0009099 | biological_process | L-valine biosynthetic process |
| F | 0016829 | molecular_function | lyase activity |
| F | 0019752 | biological_process | carboxylic acid metabolic process |
| F | 0030976 | molecular_function | thiamine pyrophosphate binding |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| G | 0000287 | molecular_function | magnesium ion binding |
| G | 0003824 | molecular_function | catalytic activity |
| G | 0003984 | molecular_function | acetolactate synthase activity |
| G | 0005948 | cellular_component | acetolactate synthase complex |
| G | 0009097 | biological_process | isoleucine biosynthetic process |
| G | 0009099 | biological_process | L-valine biosynthetic process |
| G | 0016829 | molecular_function | lyase activity |
| G | 0019752 | biological_process | carboxylic acid metabolic process |
| G | 0030976 | molecular_function | thiamine pyrophosphate binding |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| H | 0000287 | molecular_function | magnesium ion binding |
| H | 0003824 | molecular_function | catalytic activity |
| H | 0003984 | molecular_function | acetolactate synthase activity |
| H | 0005948 | cellular_component | acetolactate synthase complex |
| H | 0009097 | biological_process | isoleucine biosynthetic process |
| H | 0009099 | biological_process | L-valine biosynthetic process |
| H | 0016829 | molecular_function | lyase activity |
| H | 0019752 | biological_process | carboxylic acid metabolic process |
| H | 0030976 | molecular_function | thiamine pyrophosphate binding |
| H | 0046872 | molecular_function | metal ion binding |
| H | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 601 |
| Chain | Residue |
| A | ASP448 |
| A | MET473 |
| A | ASN475 |
| A | SER477 |
| A | TPP602 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE TPP A 602 |
| Chain | Residue |
| A | ASN419 |
| A | SER420 |
| A | MET421 |
| A | GLY447 |
| A | ASP448 |
| A | GLY449 |
| A | SER450 |
| A | TYR453 |
| A | ASN475 |
| A | SER477 |
| A | TRP478 |
| A | GLY479 |
| A | TRP480 |
| A | THR481 |
| A | MG601 |
| B | HIS26 |
| B | GLU50 |
| B | THR73 |
| B | ASN80 |
| B | GLN113 |
| A | GLY393 |
| A | GLY394 |
| A | LEU395 |
| A | THR396 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 601 |
| Chain | Residue |
| B | ASP448 |
| B | MET473 |
| B | ASN475 |
| B | SER477 |
| B | TPP602 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE TPP B 602 |
| Chain | Residue |
| A | LEU25 |
| A | HIS26 |
| A | GLU50 |
| A | THR73 |
| A | GLY76 |
| A | ASN80 |
| B | GLY393 |
| B | GLY394 |
| B | LEU395 |
| B | THR396 |
| B | ASN419 |
| B | SER420 |
| B | MET421 |
| B | GLY447 |
| B | ASP448 |
| B | GLY449 |
| B | SER450 |
| B | TYR453 |
| B | ASN475 |
| B | SER477 |
| B | TRP478 |
| B | GLY479 |
| B | TRP480 |
| B | THR481 |
| B | MG601 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 601 |
| Chain | Residue |
| C | ASP448 |
| C | MET473 |
| C | ASN475 |
| C | SER477 |
| C | TPP602 |
| site_id | AC6 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE TPP C 602 |
| Chain | Residue |
| C | GLY393 |
| C | GLY394 |
| C | LEU395 |
| C | THR396 |
| C | ASN419 |
| C | SER420 |
| C | MET421 |
| C | GLY447 |
| C | ASP448 |
| C | GLY449 |
| C | SER450 |
| C | TYR453 |
| C | ASN475 |
| C | SER477 |
| C | TRP478 |
| C | GLY479 |
| C | TRP480 |
| C | THR481 |
| C | MG601 |
| D | HIS26 |
| D | GLY27 |
| D | GLU50 |
| D | ASN80 |
| D | GLN113 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 601 |
| Chain | Residue |
| D | ASP448 |
| D | MET473 |
| D | ASN475 |
| D | SER477 |
| D | TPP602 |
| site_id | AC8 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE TPP D 602 |
| Chain | Residue |
| D | GLY394 |
| D | LEU395 |
| D | THR396 |
| D | ASN419 |
| D | SER420 |
| D | MET421 |
| D | GLY447 |
| D | ASP448 |
| D | GLY449 |
| D | SER450 |
| D | TYR453 |
| D | ASN475 |
| D | SER477 |
| D | TRP478 |
| D | GLY479 |
| D | TRP480 |
| D | THR481 |
| D | MG601 |
| C | HIS26 |
| C | GLU50 |
| C | THR73 |
| C | GLY76 |
| C | ASN80 |
| D | GLY393 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG E 601 |
| Chain | Residue |
| E | ASP448 |
| E | MET473 |
| E | ASN475 |
| E | SER477 |
| E | TPP602 |
| site_id | BC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE TPP E 602 |
| Chain | Residue |
| E | GLY393 |
| E | GLY394 |
| E | LEU395 |
| E | THR396 |
| E | ASN419 |
| E | SER420 |
| E | MET421 |
| E | GLY447 |
| E | ASP448 |
| E | GLY449 |
| E | SER450 |
| E | TYR453 |
| E | ASN475 |
| E | SER477 |
| E | TRP478 |
| E | GLY479 |
| E | TRP480 |
| E | MG601 |
| F | HIS26 |
| F | GLU50 |
| F | ASN80 |
| F | GLN113 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG F 601 |
| Chain | Residue |
| F | ASP448 |
| F | MET473 |
| F | ASN475 |
| F | SER477 |
| F | TPP602 |
| site_id | BC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE TPP F 602 |
| Chain | Residue |
| E | LEU25 |
| E | HIS26 |
| E | GLY27 |
| E | GLU50 |
| E | THR73 |
| E | ASN80 |
| E | GLN113 |
| F | GLY393 |
| F | GLY394 |
| F | LEU395 |
| F | THR396 |
| F | ASN419 |
| F | SER420 |
| F | MET421 |
| F | GLY447 |
| F | ASP448 |
| F | GLY449 |
| F | SER450 |
| F | TYR453 |
| F | ASN475 |
| F | SER477 |
| F | TRP478 |
| F | GLY479 |
| F | TRP480 |
| F | THR481 |
| F | MG601 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG G 601 |
| Chain | Residue |
| G | ASP448 |
| G | MET473 |
| G | ASN475 |
| G | SER477 |
| G | TPP602 |
| site_id | BC5 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE TPP G 602 |
| Chain | Residue |
| G | GLY393 |
| G | GLY394 |
| G | LEU395 |
| G | THR396 |
| G | ASN419 |
| G | SER420 |
| G | MET421 |
| G | GLY447 |
| G | ASP448 |
| G | GLY449 |
| G | SER450 |
| G | TYR453 |
| G | ASN475 |
| G | SER477 |
| G | TRP478 |
| G | GLY479 |
| G | TRP480 |
| G | THR481 |
| G | MG601 |
| H | HIS26 |
| H | GLY27 |
| H | GLU50 |
| H | THR73 |
| H | GLY76 |
| H | ASN80 |
| H | GLN113 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG H 601 |
| Chain | Residue |
| H | ASP448 |
| H | ASN475 |
| H | SER477 |
| H | TPP602 |
| site_id | BC7 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE TPP H 602 |
| Chain | Residue |
| G | LEU25 |
| G | HIS26 |
| G | GLU50 |
| G | GLY76 |
| G | ASN80 |
| G | GLN113 |
| H | GLY393 |
| H | GLY394 |
| H | LEU395 |
| H | THR396 |
| H | ASN419 |
| H | SER420 |
| H | MET421 |
| H | GLY447 |
| H | ASP448 |
| H | GLY449 |
| H | SER450 |
| H | TYR453 |
| H | ASN475 |
| H | SER477 |
| H | TRP478 |
| H | GLY479 |
| H | TRP480 |
| H | THR481 |
| H | MG601 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 221 |
| Chain | Residue | Details |
| A | HIS29 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU50 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLN113 | electrostatic stabiliser, hydrogen bond acceptor |
| A | ASN419 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 221 |
| Chain | Residue | Details |
| B | HIS29 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLU50 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLN113 | electrostatic stabiliser, hydrogen bond acceptor |
| B | ASN419 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 221 |
| Chain | Residue | Details |
| C | HIS29 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | GLU50 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | GLN113 | electrostatic stabiliser, hydrogen bond acceptor |
| C | ASN419 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 221 |
| Chain | Residue | Details |
| D | HIS29 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | GLU50 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | GLN113 | electrostatic stabiliser, hydrogen bond acceptor |
| D | ASN419 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA5 |
| Number of Residues | 4 |
| Details | M-CSA 221 |
| Chain | Residue | Details |
| E | HIS29 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| E | GLU50 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| E | GLN113 | electrostatic stabiliser, hydrogen bond acceptor |
| E | ASN419 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA6 |
| Number of Residues | 4 |
| Details | M-CSA 221 |
| Chain | Residue | Details |
| F | HIS29 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| F | GLU50 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| F | GLN113 | electrostatic stabiliser, hydrogen bond acceptor |
| F | ASN419 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA7 |
| Number of Residues | 4 |
| Details | M-CSA 221 |
| Chain | Residue | Details |
| G | HIS29 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| G | GLU50 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| G | GLN113 | electrostatic stabiliser, hydrogen bond acceptor |
| G | ASN419 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA8 |
| Number of Residues | 4 |
| Details | M-CSA 221 |
| Chain | Residue | Details |
| H | HIS29 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| H | GLU50 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| H | GLN113 | electrostatic stabiliser, hydrogen bond acceptor |
| H | ASN419 | electrostatic stabiliser, hydrogen bond acceptor |
