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 |
A | TYR271 | |
C | ASP301 | |
C | ARG414 | |
C | LEU571 | |
D | TYR271 | |
D | ASP301 | |
D | ARG414 | |
D | LEU571 | |
A | ASP301 | |
A | ARG414 | |
A | LEU571 | |
B | TYR271 | |
B | ASP301 | |
B | ARG414 | |
B | LEU571 | |
C | TYR271 |
site_id | SWS_FT_FI2 |
Number of Residues | 28 |
Details | BINDING: BINDING => ECO:0000269|PubMed:14623876, ECO:0000269|PubMed:19477162 |
Chain | Residue | Details |
A | ILE410 | |
B | ASP463 | |
B | GLY464 | |
B | ASN490 | |
B | THR492 | |
B | TYR561 | |
C | ILE410 | |
C | SER436 | |
C | ASP463 | |
C | GLY464 | |
C | ASN490 | |
A | SER436 | |
C | THR492 | |
C | TYR561 | |
D | ILE410 | |
D | SER436 | |
D | ASP463 | |
D | GLY464 | |
D | ASN490 | |
D | THR492 | |
D | TYR561 | |
A | ASP463 | |
A | GLY464 | |
A | ASN490 | |
A | THR492 | |
A | TYR561 | |
B | ILE410 | |
B | SER436 |
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 |