6OVT
Crystal Structure of IlvD from Mycobacterium tuberculosis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0004160 | molecular_function | dihydroxy-acid dehydratase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005886 | cellular_component | plasma membrane |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
A | 0009097 | biological_process | isoleucine biosynthetic process |
A | 0009099 | biological_process | L-valine biosynthetic process |
A | 0016829 | molecular_function | lyase activity |
A | 0016836 | molecular_function | hydro-lyase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0004160 | molecular_function | dihydroxy-acid dehydratase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005886 | cellular_component | plasma membrane |
B | 0008652 | biological_process | amino acid biosynthetic process |
B | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
B | 0009097 | biological_process | isoleucine biosynthetic process |
B | 0009099 | biological_process | L-valine biosynthetic process |
B | 0016829 | molecular_function | lyase activity |
B | 0016836 | molecular_function | hydro-lyase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0004160 | molecular_function | dihydroxy-acid dehydratase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005886 | cellular_component | plasma membrane |
C | 0008652 | biological_process | amino acid biosynthetic process |
C | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
C | 0009097 | biological_process | isoleucine biosynthetic process |
C | 0009099 | biological_process | L-valine biosynthetic process |
C | 0016829 | molecular_function | lyase activity |
C | 0016836 | molecular_function | hydro-lyase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0004160 | molecular_function | dihydroxy-acid dehydratase activity |
D | 0005515 | molecular_function | protein binding |
D | 0005886 | cellular_component | plasma membrane |
D | 0008652 | biological_process | amino acid biosynthetic process |
D | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
D | 0009097 | biological_process | isoleucine biosynthetic process |
D | 0009099 | biological_process | L-valine biosynthetic process |
D | 0016829 | molecular_function | lyase activity |
D | 0016836 | molecular_function | hydro-lyase activity |
D | 0046872 | molecular_function | metal ion binding |
D | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue MG A 601 |
Chain | Residue |
A | ASP96 |
A | ASP138 |
A | KCX139 |
A | GLU465 |
A | HOH707 |
A | HOH737 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue FES A 602 |
Chain | Residue |
A | GLY97 |
A | CYS137 |
A | ASP138 |
A | CYS214 |
A | HOH861 |
C | MET36 |
A | CYS64 |
A | SER95 |
A | ASP96 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue MG A 603 |
Chain | Residue |
A | ASP69 |
A | HOH775 |
A | HOH932 |
A | HOH936 |
A | HOH965 |
A | HOH1014 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue MG A 604 |
Chain | Residue |
A | HOH713 |
A | HOH824 |
A | HOH841 |
A | HOH1058 |
A | HOH1072 |
A | HOH1082 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue PEG A 605 |
Chain | Residue |
A | GLY354 |
A | LEU355 |
A | LEU356 |
A | HIS357 |
A | HOH945 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue MG B 601 |
Chain | Residue |
B | ASP96 |
B | ASP138 |
B | KCX139 |
B | GLU465 |
B | HOH810 |
B | HOH905 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue FES B 602 |
Chain | Residue |
B | CYS64 |
B | GLY97 |
B | CYS137 |
B | ASP138 |
B | ALA213 |
B | CYS214 |
B | HOH859 |
D | MET36 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue PEG B 603 |
Chain | Residue |
B | ILE316 |
B | GLY354 |
B | LEU355 |
B | LEU356 |
B | HIS357 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue MG B 604 |
Chain | Residue |
B | ASP69 |
B | HOH755 |
B | HOH759 |
B | HOH819 |
B | HOH898 |
B | HOH921 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue MG B 605 |
Chain | Residue |
B | HOH715 |
B | HOH842 |
B | HOH846 |
B | HOH945 |
B | HOH947 |
B | HOH956 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue FES C 601 |
Chain | Residue |
C | CYS64 |
C | GLY97 |
C | CYS137 |
C | ASP138 |
C | ALA213 |
C | CYS214 |
C | HOH840 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue PEG C 602 |
Chain | Residue |
C | ILE316 |
C | LEU355 |
C | LEU356 |
C | HIS357 |
site_id | AD4 |
Number of Residues | 6 |
Details | binding site for residue MG C 603 |
Chain | Residue |
C | ASP96 |
C | ASP138 |
C | KCX139 |
C | GLU465 |
C | HOH829 |
C | HOH926 |
site_id | AD5 |
Number of Residues | 6 |
Details | binding site for residue MG C 604 |
Chain | Residue |
C | ASP69 |
C | HOH847 |
C | HOH851 |
C | HOH869 |
C | HOH874 |
C | HOH961 |
site_id | AD6 |
Number of Residues | 6 |
Details | binding site for residue MG C 605 |
Chain | Residue |
C | HOH723 |
C | HOH802 |
C | HOH886 |
C | HOH986 |
C | HOH993 |
C | HOH1005 |
site_id | AD7 |
Number of Residues | 6 |
Details | binding site for residue MG D 601 |
Chain | Residue |
D | ASP96 |
D | ASP138 |
D | KCX139 |
D | GLU465 |
D | HOH905 |
D | HOH906 |
site_id | AD8 |
Number of Residues | 6 |
Details | binding site for residue MG D 602 |
Chain | Residue |
D | HOH770 |
D | HOH868 |
D | HOH899 |
D | HOH926 |
D | HOH964 |
D | ASP69 |
site_id | AD9 |
Number of Residues | 8 |
Details | binding site for residue FES D 603 |
Chain | Residue |
B | MET36 |
D | CYS64 |
D | GLY97 |
D | CYS137 |
D | ASP138 |
D | ALA213 |
D | CYS214 |
D | HOH922 |
site_id | AE1 |
Number of Residues | 6 |
Details | binding site for residue MG D 604 |
Chain | Residue |
A | HOH743 |
A | HOH1080 |
D | HOH727 |
D | HOH733 |
D | HOH918 |
D | HOH1002 |
site_id | AE2 |
Number of Residues | 4 |
Details | binding site for residue NA D 605 |
Chain | Residue |
D | ASP430 |
D | GLY431 |
D | ARG433 |
D | ALA434 |
Functional Information from PROSITE/UniProt
site_id | PS00626 |
Number of Residues | 11 |
Details | RCC1_2 Regulator of chromosome condensation (RCC1) signature 2. IGSGvPHLADV |
Chain | Residue | Details |
A | ILE316-VAL326 |
site_id | PS00886 |
Number of Residues | 11 |
Details | ILVD_EDD_1 Dihydroxy-acid and 6-phosphogluconate dehydratases signature 1. CDKslPGmlmA |
Chain | Residue | Details |
A | CYS137-ALA147 |
site_id | PS00887 |
Number of Residues | 12 |
Details | ILVD_EDD_2 Dihydroxy-acid and 6-phosphogluconate dehydratases signature 2. LLLTDGRFSGGT |
Chain | Residue | Details |
A | LEU483-THR494 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:31315931 |
Chain | Residue | Details |
A | SER491 | |
B | SER491 | |
C | SER491 | |
D | SER491 |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:31315931, ECO:0007744|PDB:6OVT |
Chain | Residue | Details |
A | CYS64 | |
B | ASP138 | |
B | CYS214 | |
B | GLU465 | |
C | CYS64 | |
C | ASP96 | |
C | CYS137 | |
C | ASP138 | |
C | CYS214 | |
C | GLU465 | |
D | CYS64 | |
A | ASP96 | |
D | ASP96 | |
D | CYS137 | |
D | ASP138 | |
D | CYS214 | |
D | GLU465 | |
A | CYS137 | |
A | ASP138 | |
A | CYS214 | |
A | GLU465 | |
B | CYS64 | |
B | ASP96 | |
B | CYS137 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: via carbamate group => ECO:0000269|PubMed:31315931, ECO:0007744|PDB:6OVT |
Chain | Residue | Details |
A | KCX139 | |
B | KCX139 | |
C | KCX139 | |
D | KCX139 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | MOD_RES: N-acetylproline => ECO:0007744|PubMed:21969609 |
Chain | Residue | Details |
A | PRO2 | |
B | PRO2 | |
C | PRO2 | |
D | PRO2 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: N6-carboxylysine => ECO:0000269|PubMed:31315931, ECO:0007744|PDB:6OVT |
Chain | Residue | Details |
A | KCX139 | |
B | KCX139 | |
C | KCX139 | |
D | KCX139 |