3BK9
H55A mutant of tryptophan 2,3-dioxygenase from Xanthomonas campestris
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004833 | molecular_function | tryptophan 2,3-dioxygenase activity |
A | 0006569 | biological_process | tryptophan catabolic process |
A | 0019441 | biological_process | tryptophan catabolic process to kynurenine |
A | 0019442 | biological_process | tryptophan catabolic process to acetyl-CoA |
A | 0020037 | molecular_function | heme binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0051213 | molecular_function | dioxygenase activity |
B | 0004833 | molecular_function | tryptophan 2,3-dioxygenase activity |
B | 0006569 | biological_process | tryptophan catabolic process |
B | 0019441 | biological_process | tryptophan catabolic process to kynurenine |
B | 0019442 | biological_process | tryptophan catabolic process to acetyl-CoA |
B | 0020037 | molecular_function | heme binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0051213 | molecular_function | dioxygenase activity |
C | 0004833 | molecular_function | tryptophan 2,3-dioxygenase activity |
C | 0006569 | biological_process | tryptophan catabolic process |
C | 0019441 | biological_process | tryptophan catabolic process to kynurenine |
C | 0019442 | biological_process | tryptophan catabolic process to acetyl-CoA |
C | 0020037 | molecular_function | heme binding |
C | 0046872 | molecular_function | metal ion binding |
C | 0051213 | molecular_function | dioxygenase activity |
D | 0004833 | molecular_function | tryptophan 2,3-dioxygenase activity |
D | 0006569 | biological_process | tryptophan catabolic process |
D | 0019441 | biological_process | tryptophan catabolic process to kynurenine |
D | 0019442 | biological_process | tryptophan catabolic process to acetyl-CoA |
D | 0020037 | molecular_function | heme binding |
D | 0046872 | molecular_function | metal ion binding |
D | 0051213 | molecular_function | dioxygenase activity |
E | 0004833 | molecular_function | tryptophan 2,3-dioxygenase activity |
E | 0006569 | biological_process | tryptophan catabolic process |
E | 0019441 | biological_process | tryptophan catabolic process to kynurenine |
E | 0019442 | biological_process | tryptophan catabolic process to acetyl-CoA |
E | 0020037 | molecular_function | heme binding |
E | 0046872 | molecular_function | metal ion binding |
E | 0051213 | molecular_function | dioxygenase activity |
F | 0004833 | molecular_function | tryptophan 2,3-dioxygenase activity |
F | 0006569 | biological_process | tryptophan catabolic process |
F | 0019441 | biological_process | tryptophan catabolic process to kynurenine |
F | 0019442 | biological_process | tryptophan catabolic process to acetyl-CoA |
F | 0020037 | molecular_function | heme binding |
F | 0046872 | molecular_function | metal ion binding |
F | 0051213 | molecular_function | dioxygenase activity |
G | 0004833 | molecular_function | tryptophan 2,3-dioxygenase activity |
G | 0006569 | biological_process | tryptophan catabolic process |
G | 0019441 | biological_process | tryptophan catabolic process to kynurenine |
G | 0019442 | biological_process | tryptophan catabolic process to acetyl-CoA |
G | 0020037 | molecular_function | heme binding |
G | 0046872 | molecular_function | metal ion binding |
G | 0051213 | molecular_function | dioxygenase activity |
H | 0004833 | molecular_function | tryptophan 2,3-dioxygenase activity |
H | 0006569 | biological_process | tryptophan catabolic process |
H | 0019441 | biological_process | tryptophan catabolic process to kynurenine |
H | 0019442 | biological_process | tryptophan catabolic process to acetyl-CoA |
H | 0020037 | molecular_function | heme binding |
H | 0046872 | molecular_function | metal ion binding |
H | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE TRP A 402 |
Chain | Residue |
A | PHE51 |
A | HOH793 |
A | TYR113 |
A | ARG117 |
A | SER123 |
A | SER124 |
A | GLY253 |
A | THR254 |
A | HEM401 |
A | HOH552 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE TRP B 402 |
Chain | Residue |
A | TYR24 |
B | PHE51 |
B | TYR113 |
B | ARG117 |
B | SER123 |
B | SER124 |
B | GLY253 |
B | THR254 |
B | HEM401 |
B | HOH602 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE TRP C 402 |
Chain | Residue |
C | PHE51 |
C | TYR113 |
C | ARG117 |
C | SER123 |
C | SER124 |
C | ILE248 |
C | GLY253 |
C | THR254 |
C | HEM401 |
D | TYR24 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE TRP D 402 |
Chain | Residue |
C | TYR24 |
D | PHE51 |
D | TYR113 |
D | ARG117 |
D | SER123 |
D | SER124 |
D | GLY253 |
D | THR254 |
D | HEM401 |
D | HOH621 |
site_id | AC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE TRP E 402 |
Chain | Residue |
E | PHE51 |
E | TYR113 |
E | ARG117 |
E | SER123 |
E | SER124 |
E | GLY253 |
E | THR254 |
E | HEM401 |
E | HOH642 |
F | TYR24 |
F | TYR27 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE TRP F 402 |
Chain | Residue |
F | PHE51 |
F | TYR113 |
F | ARG117 |
F | SER123 |
F | SER124 |
F | GLY253 |
F | THR254 |
F | HEM401 |
F | HOH662 |
site_id | AC7 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE TRP G 402 |
Chain | Residue |
G | PHE51 |
G | TYR113 |
G | ARG117 |
G | SER123 |
G | SER124 |
G | GLY253 |
G | THR254 |
G | HEM401 |
G | HOH663 |
H | TYR27 |
H | LEU28 |
site_id | AC8 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE TRP H 402 |
Chain | Residue |
H | PHE51 |
H | TYR113 |
H | ARG117 |
H | LEU120 |
H | SER123 |
H | SER124 |
H | ILE248 |
H | GLY253 |
H | THR254 |
H | HEM401 |
H | HOH1542 |
site_id | AC9 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE HEM A 401 |
Chain | Residue |
B | TYR24 |
A | GLN54 |
A | TRP102 |
A | SER124 |
A | GLY125 |
A | PHE126 |
A | TYR131 |
A | ARG132 |
A | HIS240 |
A | VAL244 |
A | GLY253 |
A | GLY255 |
A | GLY256 |
A | SER257 |
A | TRP402 |
A | HOH552 |
A | HOH627 |
B | ARG8 |
site_id | BC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE TRP D 403 |
Chain | Residue |
A | LYS86 |
D | ARG85 |
D | LYS92 |
D | SER221 |
D | ASP225 |
D | ASP228 |
D | HOH504 |
D | HOH813 |
D | HOH821 |
site_id | BC2 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE HEM B 401 |
Chain | Residue |
A | ARG8 |
B | SER58 |
B | TRP102 |
B | LEU105 |
B | SER124 |
B | GLY125 |
B | PHE126 |
B | TYR131 |
B | ARG132 |
B | TRP236 |
B | HIS240 |
B | VAL244 |
B | GLY253 |
B | THR254 |
B | GLY255 |
B | GLY256 |
B | SER257 |
B | LEU263 |
B | ALA266 |
B | TRP402 |
B | HOH700 |
B | HOH1541 |
site_id | BC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE TRP C 403 |
Chain | Residue |
B | LYS86 |
C | ARG85 |
C | LYS92 |
C | TYR220 |
C | SER221 |
C | ASP228 |
C | HOH521 |
C | HOH912 |
C | HOH932 |
C | HOH1094 |
site_id | BC4 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE HEM C 401 |
Chain | Residue |
C | GLN54 |
C | TRP102 |
C | SER124 |
C | GLY125 |
C | PHE126 |
C | TYR131 |
C | ARG132 |
C | TRP236 |
C | HIS240 |
C | VAL244 |
C | GLY253 |
C | GLY255 |
C | SER257 |
C | TRP402 |
C | HOH632 |
C | HOH1308 |
D | TYR24 |
site_id | BC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE TRP B 403 |
Chain | Residue |
B | ARG85 |
B | LYS92 |
B | SER221 |
B | GLU224 |
B | ASP228 |
B | HOH545 |
B | HOH644 |
B | HOH718 |
C | LYS86 |
site_id | BC6 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE HEM D 401 |
Chain | Residue |
C | ARG8 |
C | TYR24 |
D | GLN54 |
D | SER58 |
D | TRP102 |
D | LEU105 |
D | SER124 |
D | GLY125 |
D | PHE126 |
D | TYR131 |
D | ARG132 |
D | HIS240 |
D | VAL244 |
D | VAL247 |
D | GLY253 |
D | GLY255 |
D | GLY256 |
D | SER257 |
D | GLY259 |
D | LEU263 |
D | ALA266 |
D | TRP402 |
D | HOH621 |
site_id | BC7 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE TRP A 403 |
Chain | Residue |
A | ARG85 |
A | LYS92 |
A | SER221 |
A | GLU224 |
A | ASP225 |
A | ASP228 |
A | HOH537 |
A | HOH788 |
A | HOH1313 |
A | HOH1475 |
D | LYS86 |
site_id | BC8 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE HEM E 401 |
Chain | Residue |
E | PHE51 |
E | GLN54 |
E | TRP102 |
E | SER124 |
E | GLY125 |
E | PHE126 |
E | TYR131 |
E | ARG132 |
E | HIS240 |
E | VAL244 |
E | GLY253 |
E | THR254 |
E | GLY255 |
E | SER257 |
E | GLY259 |
E | TRP402 |
E | HOH642 |
E | HOH798 |
F | TYR24 |
site_id | BC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE TRP E 403 |
Chain | Residue |
E | ARG85 |
E | LYS92 |
E | SER221 |
E | ASP228 |
G | LYS86 |
G | ALA89 |
site_id | CC1 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE HEM F 401 |
Chain | Residue |
E | TYR24 |
F | GLN54 |
F | SER58 |
F | TRP102 |
F | SER124 |
F | GLY125 |
F | PHE126 |
F | TYR131 |
F | ARG132 |
F | TRP236 |
F | HIS240 |
F | VAL244 |
F | VAL247 |
F | GLY253 |
F | GLY255 |
F | GLY256 |
F | SER257 |
F | GLY259 |
F | LEU263 |
F | TRP402 |
F | HOH662 |
site_id | CC2 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE HEM G 401 |
Chain | Residue |
G | GLN54 |
G | SER58 |
G | TRP102 |
G | SER124 |
G | GLY125 |
G | PHE126 |
G | TYR131 |
G | ARG132 |
G | HIS240 |
G | VAL244 |
G | VAL247 |
G | ILE248 |
G | GLY253 |
G | GLY255 |
G | GLY256 |
G | SER257 |
G | LEU263 |
G | TRP402 |
G | HOH663 |
G | HOH1133 |
G | HOH1411 |
site_id | CC3 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE HEM H 401 |
Chain | Residue |
G | TYR24 |
H | GLN54 |
H | ALA55 |
H | SER58 |
H | TRP102 |
H | SER124 |
H | GLY125 |
H | PHE126 |
H | TYR131 |
H | ARG132 |
H | TRP236 |
H | HIS240 |
H | VAL244 |
H | VAL247 |
H | GLY253 |
H | GLY255 |
H | GLY256 |
H | SER257 |
H | GLY259 |
H | TRP402 |
H | HOH1542 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01972, ECO:0000269|PubMed:17197414, ECO:0000269|PubMed:18783250, ECO:0007744|PDB:2NW8, ECO:0007744|PDB:3BK9 |
Chain | Residue | Details |
A | PHE51 | |
B | PHE51 | |
C | PHE51 | |
D | PHE51 | |
E | PHE51 | |
F | PHE51 | |
G | PHE51 | |
H | PHE51 |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01972, ECO:0000269|PubMed:17197414, ECO:0000269|PubMed:18783250, ECO:0007744|PDB:2NW8, ECO:0007744|PDB:3BK9, ECO:0007744|PDB:3E08 |
Chain | Residue | Details |
A | TYR113 | |
D | TYR113 | |
D | ARG117 | |
D | THR254 | |
E | TYR113 | |
E | ARG117 | |
E | THR254 | |
F | TYR113 | |
F | ARG117 | |
F | THR254 | |
G | TYR113 | |
A | ARG117 | |
G | ARG117 | |
G | THR254 | |
H | TYR113 | |
H | ARG117 | |
H | THR254 | |
A | THR254 | |
B | TYR113 | |
B | ARG117 | |
B | THR254 | |
C | TYR113 | |
C | ARG117 | |
C | THR254 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: axial binding residue => ECO:0000255|HAMAP-Rule:MF_01972, ECO:0000269|PubMed:17197414, ECO:0000269|PubMed:18783250, ECO:0007744|PDB:2NW7, ECO:0007744|PDB:2NW8, ECO:0007744|PDB:2NW9, ECO:0007744|PDB:3BK9, ECO:0007744|PDB:3E08 |
Chain | Residue | Details |
A | HIS240 | |
B | HIS240 | |
C | HIS240 | |
D | HIS240 | |
E | HIS240 | |
F | HIS240 | |
G | HIS240 | |
H | HIS240 |