3QBD
3-Dehydroquinate Synthase (aroB) from Mycobacterium tuberculosis in complex with NAD
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003856 | molecular_function | 3-dehydroquinate synthase activity |
A | 0005507 | molecular_function | copper ion binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0008270 | molecular_function | zinc ion binding |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
A | 0009274 | cellular_component | peptidoglycan-based cell wall |
A | 0009423 | biological_process | chorismate biosynthetic process |
A | 0016829 | molecular_function | lyase activity |
A | 0016838 | molecular_function | carbon-oxygen lyase activity, acting on phosphates |
A | 0046872 | molecular_function | metal ion binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003856 | molecular_function | 3-dehydroquinate synthase activity |
B | 0005507 | molecular_function | copper ion binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0005886 | cellular_component | plasma membrane |
B | 0008270 | molecular_function | zinc ion binding |
B | 0008652 | biological_process | amino acid biosynthetic process |
B | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
B | 0009274 | cellular_component | peptidoglycan-based cell wall |
B | 0009423 | biological_process | chorismate biosynthetic process |
B | 0016829 | molecular_function | lyase activity |
B | 0016838 | molecular_function | carbon-oxygen lyase activity, acting on phosphates |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE NAD A 400 |
Chain | Residue |
A | GLN45 |
A | THR131 |
A | THR132 |
A | LEU134 |
A | ALA139 |
A | LYS144 |
A | ASN154 |
A | THR171 |
A | THR174 |
A | LEU175 |
A | HOH414 |
A | ASP73 |
A | ALA74 |
A | GLU75 |
A | LYS78 |
A | GLY106 |
A | GLY107 |
A | ALA108 |
A | ASP111 |
site_id | AC2 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE NAD B 400 |
Chain | Residue |
B | GLN45 |
B | ASP73 |
B | ALA74 |
B | GLU75 |
B | LYS78 |
B | GLY106 |
B | GLY107 |
B | ALA108 |
B | ASP111 |
B | THR131 |
B | THR132 |
B | LEU134 |
B | ASP138 |
B | ALA139 |
B | LYS144 |
B | ASN154 |
B | THR171 |
B | THR174 |
B | LEU175 |
B | HOH375 |
Functional Information from PROSITE/UniProt
site_id | PS00092 |
Number of Residues | 7 |
Details | N6_MTASE N-6 Adenine-specific DNA methylases signature. VAVDPPY |
Chain | Residue | Details |
A | VAL12-TYR18 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|Ref.5, ECO:0007744|PDB:3QBD |
Chain | Residue | Details |
A | GLN45 | |
B | GLN45 |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00110, ECO:0000269|Ref.5, ECO:0007744|PDB:3QBD |
Chain | Residue | Details |
A | ASP73 | |
B | THR171 | |
A | GLY107 | |
A | THR131 | |
A | LYS144 | |
A | THR171 | |
B | ASP73 | |
B | GLY107 | |
B | THR131 | |
B | LYS144 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q6GGU4, ECO:0000255|HAMAP-Rule:MF_00110 |
Chain | Residue | Details |
A | LYS153 | |
B | LYS153 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00110, ECO:0007744|PDB:3QBE |
Chain | Residue | Details |
A | GLU186 | |
A | HIS249 | |
A | HIS265 | |
B | GLU186 | |
B | HIS249 | |
B | HIS265 |