2IHU
Carboxyethylarginine synthase from Streptomyces clavuligerus: putative reaction intermediate complex
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 | TP9600 |
A | HOH1755 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE K A 602 |
Chain | Residue |
A | GLU396 |
A | GLU397 |
A | ALA399 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 601 |
Chain | Residue |
B | ASN490 |
B | THR492 |
B | TP9600 |
B | HOH868 |
B | ASP463 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K B 602 |
Chain | Residue |
B | GLU396 |
B | GLU397 |
B | ALA399 |
B | HOH898 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 601 |
Chain | Residue |
C | ASP463 |
C | ASN490 |
C | THR492 |
C | TP8600 |
C | HOH1733 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE K C 602 |
Chain | Residue |
C | GLU396 |
C | GLU397 |
C | ALA399 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 601 |
Chain | Residue |
D | ASP463 |
D | ASN490 |
D | THR492 |
D | TP9600 |
D | HOH827 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE K D 602 |
Chain | Residue |
D | GLU396 |
D | GLU397 |
D | ALA399 |
site_id | AC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE K A 1501 |
Chain | Residue |
A | HIS56 |
A | SER468 |
A | HOH1536 |
A | HOH1751 |
B | HIS56 |
B | SER468 |
B | HOH652 |
B | HOH929 |
site_id | BC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE K C 1502 |
Chain | Residue |
C | HIS56 |
C | SER468 |
C | HOH1537 |
C | HOH1723 |
D | HIS56 |
D | SER468 |
D | HOH675 |
D | HOH789 |
site_id | BC2 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE TP9 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 | TAR603 |
A | HOH1750 |
A | HOH1755 |
B | VAL34 |
B | GLY35 |
B | GLU57 |
B | THR80 |
B | PRO83 |
B | ASN87 |
site_id | BC3 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE TP9 B 600 |
Chain | Residue |
B | HOH864 |
B | HOH868 |
A | GLY35 |
A | GLU57 |
A | THR80 |
A | PRO83 |
A | ASN87 |
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 |
site_id | BC4 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE TP8 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 | ILE496 |
C | TYR499 |
C | TYR561 |
C | TP8600 |
C | MG601 |
C | HOH1676 |
C | HOH1687 |
C | HOH1733 |
C | HOH1794 |
D | GLY35 |
D | GLU57 |
D | THR80 |
D | PRO83 |
D | ASN87 |
D | HIS120 |
D | GLN121 |
site_id | BC5 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE TP8 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 | ILE496 |
C | TYR499 |
C | TYR561 |
C | TP8600 |
C | MG601 |
C | HOH1676 |
C | HOH1687 |
C | HOH1733 |
C | HOH1794 |
D | GLY35 |
D | GLU57 |
D | THR80 |
D | PRO83 |
D | ASN87 |
D | HIS120 |
D | GLN121 |
site_id | BC6 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE TP9 D 600 |
Chain | Residue |
C | VAL34 |
C | GLY35 |
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 | TAR603 |
D | HOH825 |
D | HOH827 |
site_id | BC7 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE TAR A 603 |
Chain | Residue |
A | TYR271 |
A | ILE410 |
A | ARG414 |
A | HIS415 |
A | LEU495 |
A | TP9600 |
A | HOH1581 |
A | HOH1614 |
A | HOH1615 |
B | HIS120 |
B | GLN121 |
site_id | BC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE TAR D 603 |
Chain | Residue |
C | HIS120 |
C | GLN121 |
D | TYR271 |
D | ILE410 |
D | ARG414 |
D | HIS415 |
D | SER436 |
D | LEU495 |
D | TP9600 |
D | HOH869 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 603 |
Chain | Residue |
B | ARG367 |
B | GLU370 |
B | PHE371 |
B | ASP374 |
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 |