1UPA
Carboxyethylarginine synthase from Streptomyces clavuligerus (SeMet structure)
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 | 0016740 | molecular_function | transferase activity |
| A | 0030976 | molecular_function | thiamine pyrophosphate binding |
| A | 0033848 | molecular_function | N2-(2-carboxyethyl)arginine synthase activity |
| 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 | 0016740 | molecular_function | transferase activity |
| B | 0030976 | molecular_function | thiamine pyrophosphate binding |
| B | 0033848 | molecular_function | N2-(2-carboxyethyl)arginine synthase activity |
| 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 | 0016740 | molecular_function | transferase activity |
| C | 0030976 | molecular_function | thiamine pyrophosphate binding |
| C | 0033848 | molecular_function | N2-(2-carboxyethyl)arginine synthase activity |
| 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 | 0016740 | molecular_function | transferase activity |
| D | 0030976 | molecular_function | thiamine pyrophosphate binding |
| D | 0033848 | molecular_function | N2-(2-carboxyethyl)arginine synthase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 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 | ASP463 |
| A | ASN490 |
| A | THR492 |
| A | TPP600 |
| A | HOH2210 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 602 |
| Chain | Residue |
| A | HOH2110 |
| A | HOH2190 |
| B | HIS120 |
| B | GLN121 |
| A | TYR271 |
| A | ARG414 |
| A | HIS415 |
| A | LEU495 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 603 |
| Chain | Residue |
| A | ASN490 |
| A | ASN560 |
| A | TYR561 |
| A | ASP562 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 601 |
| Chain | Residue |
| B | ASP463 |
| B | ASN490 |
| B | THR492 |
| B | TPP600 |
| B | HOH2278 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 B 602 |
| Chain | Residue |
| A | HIS120 |
| A | GLN121 |
| B | TYR271 |
| B | ARG414 |
| B | HIS415 |
| B | LEU495 |
| B | HOH2139 |
| B | HOH2279 |
| B | HOH2280 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 603 |
| Chain | Residue |
| B | ASN490 |
| B | ASN560 |
| B | TYR561 |
| B | ASP562 |
| B | PHE563 |
| B | HOH2281 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 601 |
| Chain | Residue |
| C | ASP463 |
| C | ASN490 |
| C | THR492 |
| C | TPP600 |
| C | HOH2170 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 C 602 |
| Chain | Residue |
| C | TYR271 |
| C | ARG414 |
| C | HIS415 |
| C | LEU495 |
| C | HOH2148 |
| D | HIS120 |
| D | GLN121 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 603 |
| Chain | Residue |
| C | ASN490 |
| C | ASN560 |
| C | TYR561 |
| C | ASP562 |
| C | PHE563 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 601 |
| Chain | Residue |
| D | ASP463 |
| D | ASN490 |
| D | THR492 |
| D | TPP600 |
| D | HOH2188 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 D 602 |
| Chain | Residue |
| C | HIS120 |
| C | GLN121 |
| D | TYR271 |
| D | ARG414 |
| D | HIS415 |
| D | LEU495 |
| D | HOH2098 |
| D | HOH2219 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 603 |
| Chain | Residue |
| D | ASN490 |
| D | ASN560 |
| D | TYR561 |
| D | ASP562 |
| site_id | BC4 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE TPP A 600 |
| Chain | Residue |
| A | ILE410 |
| A | GLY411 |
| A | PHE412 |
| A | PHE413 |
| A | SER436 |
| A | SER437 |
| A | PHE438 |
| A | GLY462 |
| A | ASP463 |
| A | GLY464 |
| A | GLY465 |
| A | ASN490 |
| A | THR492 |
| A | ASN493 |
| A | GLY494 |
| A | LEU495 |
| A | TYR561 |
| A | MG601 |
| A | HOH2210 |
| A | HOH2250 |
| B | GLU57 |
| B | THR80 |
| B | ASN87 |
| site_id | BC5 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE TPP B 600 |
| Chain | Residue |
| B | PHE412 |
| B | PHE413 |
| B | SER436 |
| B | SER437 |
| B | PHE438 |
| B | GLY462 |
| B | ASP463 |
| B | GLY464 |
| B | GLY465 |
| B | ASN490 |
| B | THR492 |
| B | ASN493 |
| B | GLY494 |
| B | LEU495 |
| B | TYR561 |
| B | MG601 |
| B | HOH2277 |
| B | HOH2278 |
| A | GLU57 |
| A | THR80 |
| A | ASN87 |
| B | ILE410 |
| B | GLY411 |
| site_id | BC6 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE TPP C 600 |
| Chain | Residue |
| C | ILE410 |
| C | GLY411 |
| C | PHE412 |
| C | PHE413 |
| C | SER436 |
| C | PHE438 |
| C | GLY462 |
| C | ASP463 |
| C | GLY464 |
| C | GLY465 |
| C | ASN490 |
| C | THR492 |
| C | ASN493 |
| C | GLY494 |
| C | LEU495 |
| C | TYR561 |
| C | MG601 |
| C | HOH2170 |
| C | HOH2197 |
| D | GLU57 |
| D | THR80 |
| D | ASN87 |
| site_id | BC7 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE TPP D 600 |
| Chain | Residue |
| C | GLU57 |
| C | THR80 |
| C | ASN87 |
| D | ILE410 |
| D | GLY411 |
| D | PHE412 |
| D | PHE413 |
| D | SER436 |
| D | SER437 |
| D | PHE438 |
| D | GLY462 |
| D | ASP463 |
| D | GLY464 |
| D | GLY465 |
| D | ASN490 |
| D | THR492 |
| D | ASN493 |
| D | GLY494 |
| D | LEU495 |
| D | TYR561 |
| D | MG601 |
| D | HOH2188 |
| D | HOH2217 |
Functional Information from PROSITE/UniProt
| site_id | PS00187 |
| Number of Residues | 20 |
| Details | TPP_ENZYMES Thiamine pyrophosphate enzymes signature. IGaqmarPdqptFlIaGDGG |
| Chain | Residue | Details |
| A | ILE446-GLY465 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19477162","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 56 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14623876","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19477162","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| A | PRO565 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| B | PRO565 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| D | PRO565 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 367 |
| Chain | Residue | Details |
| A | GLY61 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ARG478 | steric role |
| A | SER507 | metal ligand |
| A | THR534 | metal ligand |
| A | ARG536 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 367 |
| Chain | Residue | Details |
| B | GLY61 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ARG478 | steric role |
| B | SER507 | metal ligand |
| B | THR534 | metal ligand |
| B | ARG536 | metal ligand |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 367 |
| Chain | Residue | Details |
| C | GLY61 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | ARG478 | steric role |
| C | SER507 | metal ligand |
| C | THR534 | metal ligand |
| C | ARG536 | metal ligand |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 367 |
| Chain | Residue | Details |
| D | GLY61 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | ARG478 | steric role |
| D | SER507 | metal ligand |
| D | THR534 | metal ligand |
| D | ARG536 | metal ligand |
