3V3N
Crystal structure of TetX2 T280A: an adaptive mutant in complex with minocycline
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004497 | molecular_function | monooxygenase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0046677 | biological_process | response to antibiotic |
A | 0071949 | molecular_function | FAD binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004497 | molecular_function | monooxygenase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0046677 | biological_process | response to antibiotic |
B | 0071949 | molecular_function | FAD binding |
C | 0000166 | molecular_function | nucleotide binding |
C | 0004497 | molecular_function | monooxygenase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0046677 | biological_process | response to antibiotic |
C | 0071949 | molecular_function | FAD binding |
D | 0000166 | molecular_function | nucleotide binding |
D | 0004497 | molecular_function | monooxygenase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0046677 | biological_process | response to antibiotic |
D | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE MIY A 2001 |
Chain | Residue |
A | GLN192 |
A | FAD2004 |
A | ARG213 |
A | PHE224 |
A | PHE235 |
A | GLY236 |
A | PRO318 |
A | PHE319 |
A | GLY321 |
A | ASN371 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 2002 |
Chain | Residue |
A | GLU52 |
A | ALA53 |
A | ARG54 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 2003 |
Chain | Residue |
A | ARG137 |
A | LYS156 |
site_id | AC4 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE FAD A 2004 |
Chain | Residue |
A | ILE22 |
A | GLY23 |
A | GLY24 |
A | GLY25 |
A | PRO26 |
A | VAL27 |
A | TYR45 |
A | GLU46 |
A | ARG47 |
A | ASP48 |
A | ARG117 |
A | ARG121 |
A | ARG137 |
A | LEU139 |
A | ASN168 |
A | GLY169 |
A | GLN192 |
A | GLY310 |
A | ASP311 |
A | PRO318 |
A | GLY321 |
A | GLN322 |
A | GLY323 |
A | VAL324 |
A | MIY2001 |
A | HOH2114 |
A | HOH2128 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE MIY B 2001 |
Chain | Residue |
B | GLN192 |
B | PHE224 |
B | ALA225 |
B | HIS234 |
B | GLY236 |
B | PRO318 |
B | PHE319 |
B | ALA320 |
B | GLY321 |
B | ASN371 |
B | MET375 |
B | PHE382 |
B | FAD2004 |
B | HOH2112 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 2002 |
Chain | Residue |
B | GLU52 |
B | ARG54 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 2003 |
Chain | Residue |
B | ARG137 |
B | LYS156 |
site_id | AC8 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE FAD B 2004 |
Chain | Residue |
B | ILE22 |
B | GLY23 |
B | GLY25 |
B | PRO26 |
B | VAL27 |
B | TYR45 |
B | GLU46 |
B | ARG47 |
B | ASP48 |
B | THR59 |
B | LEU60 |
B | ARG117 |
B | ARG137 |
B | LYS138 |
B | LEU139 |
B | ASN168 |
B | GLY169 |
B | LEU287 |
B | GLY310 |
B | ASP311 |
B | PRO318 |
B | GLY321 |
B | GLN322 |
B | GLY323 |
B | VAL324 |
B | MIY2001 |
B | HOH2108 |
B | HOH2134 |
B | HOH2150 |
site_id | AC9 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE MIY C 2001 |
Chain | Residue |
C | PHE382 |
C | FAD2004 |
C | GLN192 |
C | ARG213 |
C | PHE224 |
C | HIS234 |
C | PHE235 |
C | GLY236 |
C | PRO318 |
C | PHE319 |
C | ASN371 |
C | MET375 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 C 2002 |
Chain | Residue |
C | GLU52 |
C | ARG54 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 C 2003 |
Chain | Residue |
C | ARG137 |
C | LYS156 |
site_id | BC3 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE FAD C 2004 |
Chain | Residue |
C | ILE22 |
C | GLY23 |
C | GLY25 |
C | PRO26 |
C | VAL27 |
C | TYR45 |
C | GLU46 |
C | ARG47 |
C | ASP48 |
C | LEU60 |
C | ARG117 |
C | ARG137 |
C | LEU139 |
C | ASN168 |
C | LEU287 |
C | GLY310 |
C | ASP311 |
C | PRO318 |
C | GLY321 |
C | GLN322 |
C | GLY323 |
C | VAL324 |
C | MIY2001 |
C | HOH2110 |
C | HOH2125 |
C | HOH2138 |
site_id | BC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE MIY D 2001 |
Chain | Residue |
D | GLN192 |
D | PHE224 |
D | ALA225 |
D | HIS234 |
D | GLY236 |
D | PRO318 |
D | PHE319 |
D | ALA320 |
D | GLY321 |
D | ASN371 |
D | MET375 |
D | FAD2004 |
site_id | BC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SO4 D 2002 |
Chain | Residue |
D | ARG54 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 D 2003 |
Chain | Residue |
D | ARG137 |
D | LYS156 |
site_id | BC7 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE FAD D 2004 |
Chain | Residue |
D | ILE22 |
D | GLY23 |
D | GLY25 |
D | PRO26 |
D | VAL27 |
D | TYR45 |
D | GLU46 |
D | ARG47 |
D | LEU60 |
D | ARG117 |
D | ARG137 |
D | LEU139 |
D | ASN168 |
D | GLY169 |
D | GLY310 |
D | ASP311 |
D | PRO318 |
D | GLY321 |
D | GLN322 |
D | GLY323 |
D | VAL324 |
D | MIY2001 |
D | HOH2121 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21402075, ECO:0000269|PubMed:21590745, ECO:0007744|PDB:2XDO, ECO:0007744|PDB:2XYO, ECO:0007744|PDB:2Y6Q, ECO:0007744|PDB:2Y6R, ECO:0007744|PDB:3P9U, ECO:0007744|PDB:3V3N, ECO:0007744|PDB:3V3O, ECO:0007744|PDB:4A6N, ECO:0007744|PDB:4A99, ECO:0007744|PDB:4GUV |
Chain | Residue | Details |
A | PRO26 | |
C | TYR45 | |
C | LEU139 | |
C | GLY321 | |
D | PRO26 | |
D | TYR45 | |
D | LEU139 | |
D | GLY321 | |
A | TYR45 | |
A | LEU139 | |
A | GLY321 | |
B | PRO26 | |
B | TYR45 | |
B | LEU139 | |
B | GLY321 | |
C | PRO26 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00845, ECO:0000305|PubMed:21402075 |
Chain | Residue | Details |
A | ARG54 | |
B | ARG54 | |
C | ARG54 | |
D | ARG54 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00845, ECO:0007744|PDB:3V3O |
Chain | Residue | Details |
A | ASP61 | |
B | ASP61 | |
C | ASP61 | |
D | ASP61 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00845, ECO:0000269|PubMed:21402075, ECO:0000269|PubMed:21590745, ECO:0007744|PDB:2XDO, ECO:0007744|PDB:2XYO, ECO:0007744|PDB:2Y6Q, ECO:0007744|PDB:2Y6R, ECO:0007744|PDB:3P9U, ECO:0007744|PDB:3V3N, ECO:0007744|PDB:3V3O, ECO:0007744|PDB:4A6N, ECO:0007744|PDB:4A99, ECO:0007744|PDB:4GUV |
Chain | Residue | Details |
A | ARG117 | |
A | ASP311 | |
B | ARG117 | |
B | ASP311 | |
C | ARG117 | |
C | ASP311 | |
D | ARG117 | |
D | ASP311 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21402075, ECO:0000269|PubMed:23999299, ECO:0007744|PDB:2Y6Q, ECO:0007744|PDB:2Y6R, ECO:0007744|PDB:3V3N, ECO:0007744|PDB:4A99 |
Chain | Residue | Details |
A | GLN192 | |
B | GLN192 | |
C | GLN192 | |
D | GLN192 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21402075, ECO:0000269|PubMed:23999299, ECO:0007744|PDB:2Y6Q, ECO:0007744|PDB:2Y6R, ECO:0007744|PDB:3V3O, ECO:0007744|PDB:4A6N, ECO:0007744|PDB:4A99 |
Chain | Residue | Details |
A | ARG213 | |
B | ARG213 | |
C | ARG213 | |
D | ARG213 |