2IHT
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 | 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 | 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 | 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 | 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 | HOH793 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 602 |
| Chain | Residue |
| A | HOH667 |
| A | HOH697 |
| A | HOH817 |
| A | HOH834 |
| B | HIS120 |
| B | GLN121 |
| A | TYR271 |
| A | ARG414 |
| A | HIS415 |
| A | LEU495 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 603 |
| Chain | Residue |
| A | ASN490 |
| A | ASN560 |
| A | TYR561 |
| A | ASP562 |
| A | PHE563 |
| A | HOH791 |
| 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 | HOH913 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 B 602 |
| Chain | Residue |
| A | HIS120 |
| A | GLN121 |
| A | HOH887 |
| B | TYR271 |
| B | ARG414 |
| B | HIS415 |
| B | LEU495 |
| B | HOH661 |
| B | HOH737 |
| B | HOH914 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 603 |
| Chain | Residue |
| B | ASN490 |
| B | ASN560 |
| B | TYR561 |
| B | ASP562 |
| B | PHE563 |
| B | HOH743 |
| B | HOH1038 |
| 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 | HOH834 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 C 602 |
| Chain | Residue |
| C | TYR271 |
| C | ARG414 |
| C | HIS415 |
| C | LEU495 |
| C | HOH646 |
| C | HOH856 |
| C | HOH884 |
| D | HIS120 |
| D | HOH2139 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 C 603 |
| Chain | Residue |
| C | ASN490 |
| C | ASN560 |
| C | TYR561 |
| C | ASP562 |
| C | HOH675 |
| C | HOH905 |
| 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 | HOH2106 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 D 602 |
| Chain | Residue |
| C | HIS120 |
| C | GLN121 |
| C | HOH846 |
| D | TYR271 |
| D | ARG414 |
| D | HIS415 |
| D | LEU495 |
| D | HOH1972 |
| D | HOH2001 |
| D | HOH2141 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 D 603 |
| Chain | Residue |
| D | ASN490 |
| D | ASN560 |
| D | TYR561 |
| D | ASP562 |
| D | HOH2108 |
| D | HOH2234 |
| D | HOH2277 |
| D | HOH2292 |
| site_id | BC4 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE TPP A 600 |
| Chain | Residue |
| A | ASN493 |
| A | GLY494 |
| A | LEU495 |
| A | TYR561 |
| A | MG601 |
| A | HOH610 |
| A | HOH793 |
| B | GLU57 |
| B | THR80 |
| B | PRO83 |
| B | ASN87 |
| 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 |
| site_id | BC5 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE TPP B 600 |
| Chain | Residue |
| A | GLU57 |
| A | THR80 |
| A | PRO83 |
| A | ASN87 |
| A | HOH887 |
| B | ILE410 |
| B | GLY411 |
| 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 | HOH606 |
| site_id | BC6 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE TPP C 600 |
| Chain | Residue |
| C | ILE410 |
| C | GLY411 |
| C | PHE412 |
| C | PHE413 |
| C | SER436 |
| C | SER437 |
| 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 | HOH618 |
| D | GLU57 |
| D | THR80 |
| D | ASN87 |
| D | HOH2139 |
| site_id | BC7 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE TPP D 600 |
| Chain | Residue |
| C | GLU57 |
| C | THR80 |
| C | PRO83 |
| 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 | HOH1910 |
| D | HOH2106 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 604 |
| Chain | Residue |
| A | GLU370 |
| A | HIS385 |
| A | HOH901 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 604 |
| Chain | Residue |
| B | GLU370 |
| B | PHE371 |
| B | ASP374 |
| B | HIS385 |
| B | HOH1045 |
| B | HOH1087 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL D 604 |
| Chain | Residue |
| D | GLU370 |
| D | ASP374 |
| D | HIS385 |
| D | HOH2281 |
| D | HOH2313 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL D 1905 |
| Chain | Residue |
| D | HOH1911 |
| D | HOH2024 |
| D | HOH2026 |
| D | HOH2123 |
| D | HOH2311 |
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 | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19477162 |
| Chain | Residue | Details |
| C | TYR271 | |
| C | ASP301 | |
| C | ARG414 | |
| C | LEU571 | |
| D | TYR271 | |
| D | ASP301 | |
| D | ARG414 | |
| D | LEU571 | |
| A | TYR271 | |
| A | ASP301 | |
| A | ARG414 | |
| A | LEU571 | |
| B | TYR271 | |
| B | ASP301 | |
| B | ARG414 | |
| B | LEU571 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14623876, ECO:0000269|PubMed:19477162 |
| Chain | Residue | Details |
| A | ASN490 | |
| A | THR492 | |
| A | TYR561 | |
| B | ILE410 | |
| B | SER436 | |
| B | ASP463 | |
| B | GLY464 | |
| B | ASN490 | |
| B | THR492 | |
| B | TYR561 | |
| C | ILE410 | |
| C | SER436 | |
| C | ASP463 | |
| C | GLY464 | |
| C | ASN490 | |
| C | THR492 | |
| C | TYR561 | |
| D | ILE410 | |
| D | SER436 | |
| D | ASP463 | |
| D | GLY464 | |
| D | ASN490 | |
| D | THR492 | |
| D | TYR561 | |
| A | ILE410 | |
| A | SER436 | |
| A | ASP463 | |
| A | GLY464 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 367 |
| Chain | Residue | Details |
| A | GLU57 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | PHE438 | steric role |
| A | ASP463 | metal ligand |
| A | ASN490 | metal ligand |
| A | THR492 | metal ligand |
| A | TYR561 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 367 |
| Chain | Residue | Details |
| B | GLU57 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | PHE438 | steric role |
| B | ASP463 | metal ligand |
| B | ASN490 | metal ligand |
| B | THR492 | metal ligand |
| B | TYR561 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA3 |
| Number of Residues | 6 |
| Details | M-CSA 367 |
| Chain | Residue | Details |
| C | GLU57 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | PHE438 | steric role |
| C | ASP463 | metal ligand |
| C | ASN490 | metal ligand |
| C | THR492 | metal ligand |
| C | TYR561 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA4 |
| Number of Residues | 6 |
| Details | M-CSA 367 |
| Chain | Residue | Details |
| D | GLU57 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | PHE438 | steric role |
| D | ASP463 | metal ligand |
| D | ASN490 | metal ligand |
| D | THR492 | metal ligand |
| D | TYR561 | electrostatic stabiliser, hydrogen bond acceptor |
