1P3W
X-ray crystal structure of E. coli IscS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0002143 | biological_process | tRNA wobble position uridine thiolation |
| A | 0002937 | biological_process | tRNA 4-thiouridine biosynthesis |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008033 | biological_process | tRNA processing |
| A | 0009000 | molecular_function | selenocysteine lyase activity |
| A | 0009228 | biological_process | thiamine biosynthetic process |
| A | 0009589 | biological_process | detection of UV |
| A | 0016226 | biological_process | iron-sulfur cluster assembly |
| A | 0016261 | biological_process | selenocysteine catabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019448 | biological_process | L-cysteine catabolic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0031071 | molecular_function | cysteine desulfurase activity |
| A | 0044571 | biological_process | [2Fe-2S] cluster assembly |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| A | 0072348 | biological_process | sulfur compound transport |
| A | 0097163 | molecular_function | sulfur carrier activity |
| A | 1990221 | cellular_component | L-cysteine desulfurase complex |
| B | 0002143 | biological_process | tRNA wobble position uridine thiolation |
| B | 0002937 | biological_process | tRNA 4-thiouridine biosynthesis |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008033 | biological_process | tRNA processing |
| B | 0009000 | molecular_function | selenocysteine lyase activity |
| B | 0009228 | biological_process | thiamine biosynthetic process |
| B | 0009589 | biological_process | detection of UV |
| B | 0016226 | biological_process | iron-sulfur cluster assembly |
| B | 0016261 | biological_process | selenocysteine catabolic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0019448 | biological_process | L-cysteine catabolic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0031071 | molecular_function | cysteine desulfurase activity |
| B | 0044571 | biological_process | [2Fe-2S] cluster assembly |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| B | 0072348 | biological_process | sulfur compound transport |
| B | 0097163 | molecular_function | sulfur carrier activity |
| B | 1990221 | cellular_component | L-cysteine desulfurase complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP B 764 |
| Chain | Residue |
| A | THR243 |
| B | GLN183 |
| B | SER203 |
| B | HIS205 |
| B | LYS206 |
| B | HOH795 |
| B | HOH848 |
| B | HOH925 |
| A | HOH880 |
| B | ALA75 |
| B | THR76 |
| B | HIS104 |
| B | MET151 |
| B | ASN155 |
| B | ASP180 |
| B | THR182 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP A 764 |
| Chain | Residue |
| A | ALA75 |
| A | THR76 |
| A | HIS104 |
| A | MET151 |
| A | ASN155 |
| A | ASP180 |
| A | THR182 |
| A | GLN183 |
| A | SER203 |
| A | HIS205 |
| A | LYS206 |
| A | HOH801 |
| A | HOH823 |
| A | HOH895 |
| B | THR243 |
Functional Information from PROSITE/UniProt
| site_id | PS00595 |
| Number of Residues | 20 |
| Details | AA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. VDLMsfSGHKiygpk.GiGaL |
| Chain | Residue | Details |
| B | VAL197-LEU216 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00331","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00331","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12860127","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"HAMAP-Rule","id":"MF_00331","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12860127","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ecx |
| Chain | Residue | Details |
| A | TRP45 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ecx |
| Chain | Residue | Details |
| B | TRP45 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ecx |
| Chain | Residue | Details |
| B | HIS104 | |
| B | LYS206 | |
| B | ASP180 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ecx |
| Chain | Residue | Details |
| A | HIS104 | |
| A | LYS206 | |
| A | ASP180 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ecx |
| Chain | Residue | Details |
| B | LYS206 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ecx |
| Chain | Residue | Details |
| A | LYS206 |
