3ROI
2.20 Angstrom resolution structure of 3-phosphoshikimate 1-carboxyvinyltransferase (AroA) from Coxiella burnetii
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0003866 | molecular_function | 3-phosphoshikimate 1-carboxyvinyltransferase activity |
A | 0005737 | cellular_component | cytoplasm |
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 | 0016740 | molecular_function | transferase activity |
A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
B | 0003824 | molecular_function | catalytic activity |
B | 0003866 | molecular_function | 3-phosphoshikimate 1-carboxyvinyltransferase activity |
B | 0005737 | cellular_component | cytoplasm |
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 | 0016740 | molecular_function | transferase activity |
B | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 439 |
Chain | Residue |
A | MET45 |
A | ASN70 |
A | PHE415 |
A | PRO416 |
A | ASN417 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 440 |
Chain | Residue |
A | THR96 |
A | ARG123 |
A | LYS21 |
A | ASN93 |
A | SER94 |
A | GLY95 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 441 |
Chain | Residue |
A | ARG406 |
A | ASN407 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 442 |
Chain | Residue |
A | THR262 |
A | ARG263 |
A | LEU264 |
A | GLN309 |
A | LEU312 |
A | HOH566 |
B | LYS271 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 443 |
Chain | Residue |
A | GLY143 |
B | LYS330 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 444 |
Chain | Residue |
A | HIS160 |
A | GLY183 |
A | LYS184 |
A | HOH489 |
B | LYS222 |
B | LYS224 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 445 |
Chain | Residue |
A | LYS356 |
A | ASN381 |
A | ARG406 |
B | GLN58 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 446 |
Chain | Residue |
A | ARG99 |
A | ARG123 |
A | ARG127 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 447 |
Chain | Residue |
A | SER22 |
A | ARG26 |
A | THR96 |
A | GLN169 |
A | HOH520 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 448 |
Chain | Residue |
A | GLY329 |
A | LYS330 |
A | GLN371 |
A | HOH567 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 449 |
Chain | Residue |
A | HIS297 |
A | ARG299 |
A | HOH561 |
A | HOH572 |
B | ARG299 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 450 |
Chain | Residue |
A | ASP68 |
A | PRO124 |
A | LYS126 |
A | ARG127 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL B 439 |
Chain | Residue |
B | MET45 |
B | ASN70 |
B | PHE415 |
B | PRO416 |
B | ASN417 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL B 440 |
Chain | Residue |
B | SER172 |
B | ARG194 |
B | HIS196 |
B | THR197 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL B 441 |
Chain | Residue |
B | SER167 |
B | ALA168 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 442 |
Chain | Residue |
A | LYS271 |
B | THR262 |
B | ARG263 |
B | LEU264 |
B | GLN309 |
site_id | BC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 B 443 |
Chain | Residue |
B | SER22 |
B | ARG26 |
B | THR96 |
B | ARG99 |
B | GLN169 |
B | ARG194 |
B | HOH505 |
site_id | BC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 444 |
Chain | Residue |
A | LYS222 |
B | LYS184 |
site_id | CC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 445 |
Chain | Residue |
B | ARG99 |
B | ARG123 |
B | GLN169 |
site_id | CC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 B 446 |
Chain | Residue |
B | ASN93 |
B | SER94 |
B | GLY95 |
B | THR96 |
B | ARG99 |
B | ARG123 |
B | HOH452 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00210 |
Chain | Residue | Details |
A | ASP315 | |
B | ASP315 |
site_id | SWS_FT_FI2 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000269|Ref.4, ECO:0007744|PDB:4EGR |
Chain | Residue | Details |
A | LYS21 | |
B | THR96 | |
B | ARG123 | |
B | GLN169 | |
B | ARG346 | |
B | ARG387 | |
A | GLY95 | |
A | THR96 | |
A | ARG123 | |
A | GLN169 | |
A | ARG346 | |
A | ARG387 | |
B | LYS21 | |
B | GLY95 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|Ref.3, ECO:0000269|Ref.7, ECO:0007744|PDB:3SLH, ECO:0007744|PDB:4ZND |
Chain | Residue | Details |
A | SER22 | |
B | ALA168 | |
B | ASP315 | |
B | LYS342 | |
A | ARG26 | |
A | SER167 | |
A | ALA168 | |
A | ASP315 | |
A | LYS342 | |
B | SER22 | |
B | ARG26 | |
B | SER167 |