2NXW
Crystal structure of phenylpyruvate decarboxylase of Azospirillum brasilense
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0000949 | biological_process | aromatic amino acid family catabolic process to alcohol via Ehrlich pathway |
A | 0003824 | molecular_function | catalytic activity |
A | 0004737 | molecular_function | pyruvate decarboxylase activity |
A | 0005829 | cellular_component | cytosol |
A | 0009851 | biological_process | auxin biosynthetic process |
A | 0016831 | molecular_function | carboxy-lyase activity |
A | 0019752 | biological_process | carboxylic acid metabolic process |
A | 0030976 | molecular_function | thiamine pyrophosphate binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0047434 | molecular_function | indolepyruvate decarboxylase activity |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0000949 | biological_process | aromatic amino acid family catabolic process to alcohol via Ehrlich pathway |
B | 0003824 | molecular_function | catalytic activity |
B | 0004737 | molecular_function | pyruvate decarboxylase activity |
B | 0005829 | cellular_component | cytosol |
B | 0009851 | biological_process | auxin biosynthetic process |
B | 0016831 | molecular_function | carboxy-lyase activity |
B | 0019752 | biological_process | carboxylic acid metabolic process |
B | 0030976 | molecular_function | thiamine pyrophosphate binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0047434 | molecular_function | indolepyruvate decarboxylase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 4001 |
Chain | Residue |
B | ASP429 |
B | ASN456 |
B | SER458 |
B | TPP2001 |
B | HOH4005 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 4002 |
Chain | Residue |
A | HOH4004 |
A | ASP429 |
A | ASN456 |
A | SER458 |
A | TPP2002 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 4003 |
Chain | Residue |
A | CYS210 |
A | VAL211 |
A | THR236 |
A | ILE279 |
A | TYR400 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL B 4004 |
Chain | Residue |
B | CYS210 |
B | VAL211 |
B | THR236 |
B | ILE279 |
B | TYR400 |
site_id | AC5 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE TPP B 2001 |
Chain | Residue |
A | PRO23 |
A | GLY24 |
A | GLU48 |
B | ASP382 |
B | ALA402 |
B | MET404 |
B | GLY428 |
B | ASP429 |
B | GLY430 |
B | ALA431 |
B | ASN456 |
B | SER458 |
B | TRP459 |
B | GLU460 |
B | MET461 |
B | LEU462 |
B | MG4001 |
B | HOH4005 |
B | HOH4026 |
B | HOH4052 |
B | HOH4081 |
B | HOH4450 |
site_id | AC6 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE TPP A 2002 |
Chain | Residue |
A | ASP382 |
A | ALA402 |
A | MET404 |
A | GLY428 |
A | ASP429 |
A | GLY430 |
A | ALA431 |
A | ASN456 |
A | SER458 |
A | TRP459 |
A | GLU460 |
A | MET461 |
A | LEU462 |
A | MG4002 |
A | HOH4004 |
A | HOH4006 |
A | HOH4014 |
A | HOH4091 |
A | HOH4241 |
B | PRO23 |
B | GLY24 |
B | GLU48 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 3001 |
Chain | Residue |
B | SER63 |
B | THR64 |
B | PRO92 |
B | ARG153 |
B | SER156 |
B | ARG215 |
B | HOH4043 |
B | HOH4086 |
B | HOH4248 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 3002 |
Chain | Residue |
A | SER63 |
A | THR64 |
A | PRO92 |
A | ARG153 |
A | SER156 |
A | HOH4057 |
A | HOH4112 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 3003 |
Chain | Residue |
B | HIS43 |
B | GLN415 |
B | CYS416 |
B | LEU445 |
B | GLY446 |
B | HOH4039 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | GLU48 | |
A | ASP429 | |
A | ASN456 | |
B | GLU48 | |
B | ASP429 | |
B | ASN456 |