2OGA
X-ray crystal structure of S. venezuelae DesV in complex with ketimine intermediate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000271 | biological_process | polysaccharide biosynthetic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0033068 | biological_process | macrolide biosynthetic process |
| B | 0000271 | biological_process | polysaccharide biosynthetic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0033068 | biological_process | macrolide biosynthetic process |
| C | 0000271 | biological_process | polysaccharide biosynthetic process |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0017000 | biological_process | antibiotic biosynthetic process |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0033068 | biological_process | macrolide biosynthetic process |
| D | 0000271 | biological_process | polysaccharide biosynthetic process |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0017000 | biological_process | antibiotic biosynthetic process |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0033068 | biological_process | macrolide biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 380 |
| Chain | Residue |
| A | TYR39 |
| A | LEU40 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 380 |
| Chain | Residue |
| A | HOH1181 |
| B | TYR39 |
| B | LEU40 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL C 380 |
| Chain | Residue |
| C | ARG38 |
| C | TYR39 |
| C | LEU40 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL D 380 |
| Chain | Residue |
| D | LEU40 |
| D | TYR39 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA C 1025 |
| Chain | Residue |
| C | ASN65 |
| C | HOH1042 |
| D | ASN65 |
| D | HOH1026 |
| D | HOH1027 |
| D | HOH1028 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 1022 |
| Chain | Residue |
| A | ASN65 |
| A | HOH1040 |
| A | HOH1041 |
| A | HOH1043 |
| B | ASN65 |
| B | HOH1024 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1023 |
| Chain | Residue |
| A | TYR55 |
| A | GLU57 |
| A | ARG172 |
| A | ARG177 |
| A | HOH1124 |
| D | ASP308 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 381 |
| Chain | Residue |
| B | PRO191 |
| B | LYS193 |
| B | ASN194 |
| B | PRO355 |
| B | HOH1064 |
| B | HOH1065 |
| B | HOH1103 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO C 1026 |
| Chain | Residue |
| A | ARG224 |
| C | HIS60 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 1024 |
| Chain | Residue |
| A | PRO191 |
| A | LYS193 |
| A | ASN194 |
| A | PRO355 |
| A | HOH1068 |
| A | HOH1106 |
| A | HOH1287 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 382 |
| Chain | Residue |
| B | ARG172 |
| B | ARG177 |
| B | ASP254 |
| B | HOH1061 |
| B | HOH1259 |
| site_id | BC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PGU A 1020 |
| Chain | Residue |
| A | SER66 |
| A | GLY67 |
| A | TYR93 |
| A | ALA95 |
| A | ASP164 |
| A | ALA166 |
| A | GLN167 |
| A | SER188 |
| A | TYR190 |
| A | LYS193 |
| A | TYR318 |
| A | HOH1069 |
| A | HOH1290 |
| B | TYR221 |
| B | TYR227 |
| B | ASN235 |
| B | ARG237 |
| site_id | BC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PGU B 1021 |
| Chain | Residue |
| A | TYR221 |
| A | LYS226 |
| A | TYR227 |
| A | ASN235 |
| A | ARG237 |
| B | SER66 |
| B | GLY67 |
| B | TYR93 |
| B | ALA95 |
| B | ASP164 |
| B | ALA166 |
| B | GLN167 |
| B | SER188 |
| B | TYR190 |
| B | LYS193 |
| B | TYR318 |
| B | HOH1066 |
| B | HOH1200 |
| site_id | BC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PGU C 1023 |
| Chain | Residue |
| D | TYR227 |
| D | ASN235 |
| D | ARG237 |
| C | SER66 |
| C | GLY67 |
| C | MET68 |
| C | TYR93 |
| C | ASP164 |
| C | ALA166 |
| C | GLN167 |
| C | SER188 |
| C | TYR190 |
| C | LYS193 |
| C | TYR318 |
| C | HOH1060 |
| C | HOH1247 |
| C | HOH1248 |
| D | TYR221 |
| site_id | BC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE PGU D 1024 |
| Chain | Residue |
| C | TYR221 |
| C | TYR227 |
| C | ASN235 |
| C | ARG237 |
| D | SER66 |
| D | GLY67 |
| D | MET68 |
| D | TYR93 |
| D | ALA95 |
| D | ASP164 |
| D | ALA166 |
| D | GLN167 |
| D | SER188 |
| D | TYR190 |
| D | LYS193 |
| D | TYR318 |
| D | HOH1102 |
| D | HOH1139 |
| D | HOH1218 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17456741 |
| Chain | Residue | Details |
| A | GLY67 | |
| B | SER188 | |
| B | TYR221 | |
| B | TYR227 | |
| B | ASN235 | |
| B | TYR318 | |
| C | GLY67 | |
| C | GLN167 | |
| C | SER188 | |
| C | TYR221 | |
| C | TYR227 | |
| A | GLN167 | |
| C | ASN235 | |
| C | TYR318 | |
| D | GLY67 | |
| D | GLN167 | |
| D | SER188 | |
| D | TYR221 | |
| D | TYR227 | |
| D | ASN235 | |
| D | TYR318 | |
| A | SER188 | |
| A | TYR221 | |
| A | TYR227 | |
| A | ASN235 | |
| A | TYR318 | |
| B | GLY67 | |
| B | GLN167 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000305|PubMed:17456741 |
| Chain | Residue | Details |
| A | LYS193 | |
| B | LYS193 | |
| C | LYS193 | |
| D | LYS193 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| D | ARG38 | |
| C | ASP164 | |
| C | TYR93 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| C | ARG38 | |
| D | ASP164 | |
| D | TYR93 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ASP164 | |
| A | LYS193 | |
| A | TYR93 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | ASP164 | |
| B | LYS193 | |
| B | TYR93 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| C | ASP164 | |
| C | LYS193 | |
| C | TYR93 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| D | ASP164 | |
| D | LYS193 | |
| D | TYR93 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ASP164 | |
| A | TYR93 | |
| B | ARG38 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ARG38 | |
| B | ASP164 | |
| B | TYR93 |
