4FQ8
Crystal Structure of Shikimate Dehydrogenase (aroE) Y210A Mutant from Helicobacter pylori in Complex with Shikimate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004764 | molecular_function | shikimate 3-dehydrogenase (NADP+) activity |
A | 0005829 | cellular_component | cytosol |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
A | 0009423 | biological_process | chorismate biosynthetic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0019632 | biological_process | shikimate metabolic process |
A | 0050661 | molecular_function | NADP binding |
B | 0004764 | molecular_function | shikimate 3-dehydrogenase (NADP+) activity |
B | 0005829 | cellular_component | cytosol |
B | 0008652 | biological_process | amino acid biosynthetic process |
B | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
B | 0009423 | biological_process | chorismate biosynthetic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0019632 | biological_process | shikimate metabolic process |
B | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SKM A 500 |
Chain | Residue |
A | SER16 |
A | SER18 |
A | ASN63 |
A | VAL64 |
A | THR65 |
A | LYS69 |
A | ASN90 |
A | ASP105 |
A | GLN237 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SKM B 500 |
Chain | Residue |
B | SER16 |
B | SER18 |
B | ASN63 |
B | THR65 |
B | LYS69 |
B | ASN90 |
B | ASP105 |
B | GLN237 |
B | HOH612 |
B | HOH624 |
B | HOH637 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000305|Ref.2, ECO:0000305|Ref.3 |
Chain | Residue | Details |
A | LYS69 | |
B | LYS69 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000269|Ref.2, ECO:0000269|Ref.3, ECO:0000269|Ref.4 |
Chain | Residue | Details |
A | SER16 | |
A | THR65 | |
A | GLN237 | |
B | SER16 | |
B | THR65 | |
B | GLN237 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000269|Ref.2, ECO:0000269|Ref.3 |
Chain | Residue | Details |
A | ASN90 | |
A | ASP105 | |
B | ASN90 | |
B | ASP105 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000269|Ref.2 |
Chain | Residue | Details |
A | GLY125 | |
A | GLY230 | |
B | GLY125 | |
B | GLY230 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|Ref.2 |
Chain | Residue | Details |
A | SER181 | |
B | SER181 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00222 |
Chain | Residue | Details |
A | LEU208 | |
B | LEU208 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000269|Ref.2, ECO:0000269|Ref.4 |
Chain | Residue | Details |
A | ALA210 | |
B | ALA210 |