2OA1
Crystal Structure of RebH, a FAD-dependent halogenase from Lechevalieria aerocolonigenes, the L-Tryptophan with FAD complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0004497 | molecular_function | monooxygenase activity |
A | 0016491 | molecular_function | oxidoreductase activity |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0004497 | molecular_function | monooxygenase activity |
B | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 2001 |
Chain | Residue |
A | PRO355 |
A | THR359 |
A | GLY360 |
A | FAD2004 |
A | HOH2120 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE TRP A 2002 |
Chain | Residue |
A | PHE111 |
A | GLU357 |
A | TYR454 |
A | TYR455 |
A | GLU461 |
A | PHE465 |
A | TRP466 |
A | ASN470 |
A | HOH2124 |
A | HOH2139 |
A | ILE52 |
A | PRO53 |
A | ILE82 |
A | HIS109 |
site_id | AC3 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE TRP A 2003 |
Chain | Residue |
A | HOH2037 |
A | HOH2071 |
B | ILE52 |
B | PRO53 |
B | ILE82 |
B | HIS109 |
B | SER110 |
B | PHE111 |
B | GLU357 |
B | TYR454 |
B | TYR455 |
B | GLU461 |
B | PHE465 |
B | TRP466 |
site_id | AC4 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE FAD A 2004 |
Chain | Residue |
A | GLY12 |
A | GLY13 |
A | THR15 |
A | ALA16 |
A | GLN38 |
A | ALA39 |
A | ASP41 |
A | GLU49 |
A | ALA50 |
A | ASP195 |
A | ARG196 |
A | VAL197 |
A | CYS227 |
A | SER228 |
A | GLY229 |
A | ILE286 |
A | PHE330 |
A | THR348 |
A | PHE352 |
A | PRO355 |
A | GLY360 |
A | ILE361 |
A | CL2001 |
A | HOH2016 |
A | HOH2036 |
A | HOH2082 |
A | HOH2089 |
A | HOH2103 |
A | HOH2116 |
A | HOH2258 |
A | HOH2358 |
A | HOH2481 |
site_id | AC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE ADN B 2005 |
Chain | Residue |
B | GLY12 |
B | GLY13 |
B | ALA39 |
B | ASP41 |
B | ASP195 |
B | ARG196 |
B | VAL197 |
B | CYS227 |
B | SER228 |
B | ARG231 |
B | LEU233 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:17260957 |
Chain | Residue | Details |
A | LYS79 | |
B | LYS79 |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17260957, ECO:0000269|PubMed:17876823, ECO:0007744|PDB:2OA1, ECO:0007744|PDB:2OAL |
Chain | Residue | Details |
A | GLY13 | |
B | GLY13 | |
B | ALA16 | |
B | ALA39 | |
B | ASP41 | |
B | GLU49 | |
B | ALA50 | |
B | VAL197 | |
B | THR348 | |
B | ILE361 | |
A | ALA16 | |
A | ALA39 | |
A | ASP41 | |
A | GLU49 | |
A | ALA50 | |
A | VAL197 | |
A | THR348 | |
A | ILE361 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17260957, ECO:0007744|PDB:2OAL |
Chain | Residue | Details |
A | THR15 | |
B | THR15 |
site_id | SWS_FT_FI4 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17260957, ECO:0000269|PubMed:17876823, ECO:0007744|PDB:2E4G, ECO:0007744|PDB:2OA1 |
Chain | Residue | Details |
A | GLU357 | |
B | PHE465 | |
A | TYR454 | |
A | TYR455 | |
A | GLU461 | |
A | PHE465 | |
B | GLU357 | |
B | TYR454 | |
B | TYR455 | |
B | GLU461 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17876823, ECO:0007744|PDB:2OA1 |
Chain | Residue | Details |
A | THR359 | |
A | GLY360 | |
B | THR359 | |
B | GLY360 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | SITE: Important for activity => ECO:0000250|UniProtKB:P95480 |
Chain | Residue | Details |
A | GLU357 | |
B | GLU357 |