4WSH
Crystal structure of Probable Uroporphyrinogen decarboxylase (UPD) (URO-D) from Pseudomonas aeruginosa
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004853 | molecular_function | uroporphyrinogen decarboxylase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006778 | biological_process | porphyrin-containing compound metabolic process |
A | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
A | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
A | 0006783 | biological_process | heme biosynthetic process |
A | 0016831 | molecular_function | carboxy-lyase activity |
A | 0019353 | biological_process | protoporphyrinogen IX biosynthetic process from glutamate |
B | 0004853 | molecular_function | uroporphyrinogen decarboxylase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006778 | biological_process | porphyrin-containing compound metabolic process |
B | 0006779 | biological_process | porphyrin-containing compound biosynthetic process |
B | 0006782 | biological_process | protoporphyrinogen IX biosynthetic process |
B | 0006783 | biological_process | heme biosynthetic process |
B | 0016831 | molecular_function | carboxy-lyase activity |
B | 0019353 | biological_process | protoporphyrinogen IX biosynthetic process from glutamate |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue CL A 400 |
Chain | Residue |
A | ILE276 |
A | ASN292 |
A | ARG311 |
A | HOH662 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue SO4 A 401 |
Chain | Residue |
A | GLY355 |
A | HOH637 |
A | PRO17 |
A | VAL18 |
A | GLY319 |
A | THR320 |
A | HIS354 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue SO4 A 402 |
Chain | Residue |
A | ARG27 |
A | GLY30 |
A | ARG31 |
A | PRO332 |
A | HOH606 |
A | HOH663 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue SO4 A 403 |
Chain | Residue |
A | ARG237 |
A | GLU238 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 404 |
Chain | Residue |
A | SER106 |
A | LEU107 |
A | ASN175 |
A | HOH667 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 405 |
Chain | Residue |
A | GLN16 |
A | ARG243 |
A | HOH703 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 406 |
Chain | Residue |
A | ARG8 |
A | HOH621 |
B | ARG11 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 407 |
Chain | Residue |
A | ARG27 |
A | HIS328 |
A | GLY329 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue CL B 400 |
Chain | Residue |
B | ILE276 |
B | ASN292 |
B | ARG311 |
B | HOH532 |
site_id | AD1 |
Number of Residues | 8 |
Details | binding site for residue SO4 B 401 |
Chain | Residue |
B | PRO17 |
B | VAL18 |
B | GLY319 |
B | THR320 |
B | HIS354 |
B | GLY355 |
B | HOH604 |
B | HOH631 |
site_id | AD2 |
Number of Residues | 8 |
Details | binding site for residue SO4 B 402 |
Chain | Residue |
B | ARG27 |
B | GLY30 |
B | ARG31 |
B | PRO332 |
B | HOH558 |
B | HOH606 |
B | HOH632 |
B | HOH664 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00218 |
Chain | Residue | Details |
A | ARG27 | |
B | TYR155 | |
B | SER210 | |
B | HIS328 | |
A | PHE46 | |
A | ASP78 | |
A | TYR155 | |
A | SER210 | |
A | HIS328 | |
B | ARG27 | |
B | PHE46 | |
B | ASP78 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00218 |
Chain | Residue | Details |
A | ASP78 | |
B | ASP78 |