3S2W
The crystal structure of a MarR transcriptional regulator from Methanosarcina mazei Go1
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003700 | molecular_function | DNA-binding transcription factor activity |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
B | 0003700 | molecular_function | DNA-binding transcription factor activity |
B | 0006355 | biological_process | regulation of DNA-templated transcription |
C | 0003700 | molecular_function | DNA-binding transcription factor activity |
C | 0006355 | biological_process | regulation of DNA-templated transcription |
D | 0003700 | molecular_function | DNA-binding transcription factor activity |
D | 0006355 | biological_process | regulation of DNA-templated transcription |
E | 0003700 | molecular_function | DNA-binding transcription factor activity |
E | 0006355 | biological_process | regulation of DNA-templated transcription |
F | 0003700 | molecular_function | DNA-binding transcription factor activity |
F | 0006355 | biological_process | regulation of DNA-templated transcription |
G | 0003700 | molecular_function | DNA-binding transcription factor activity |
G | 0006355 | biological_process | regulation of DNA-templated transcription |
H | 0003700 | molecular_function | DNA-binding transcription factor activity |
H | 0006355 | biological_process | regulation of DNA-templated transcription |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 157 |
Chain | Residue |
A | GLY46 |
A | SER47 |
A | GLY48 |
A | GLN49 |
A | LYS84 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 158 |
Chain | Residue |
A | GLY76 |
A | ARG80 |
C | ARG95 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 159 |
Chain | Residue |
A | ILE128 |
B | LYS120 |
B | GLU124 |
A | TYR35 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 157 |
Chain | Residue |
B | GLY46 |
B | SER47 |
B | GLY48 |
B | GLN49 |
B | LYS84 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 C 157 |
Chain | Residue |
C | GLY46 |
C | SER47 |
C | GLY48 |
C | GLN49 |
C | LYS84 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 C 158 |
Chain | Residue |
C | ASN63 |
C | SER66 |
C | ARG104 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 D 157 |
Chain | Residue |
D | GLY46 |
D | SER47 |
D | GLY48 |
D | GLN49 |
D | LYS84 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 D 158 |
Chain | Residue |
C | GLU140 |
D | ARG136 |
D | GLN137 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 E 157 |
Chain | Residue |
E | GLY46 |
E | SER47 |
E | GLY48 |
E | GLN49 |
E | LYS84 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 F 157 |
Chain | Residue |
F | ASP74 |
F | LYS75 |
H | ARG104 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 F 158 |
Chain | Residue |
F | ARG95 |
F | SER102 |
H | GLN94 |
H | ARG95 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 G 157 |
Chain | Residue |
G | TYR29 |
H | TYR29 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 G 158 |
Chain | Residue |
E | THR108 |
E | GLU109 |
E | LYS110 |
G | ARG80 |
G | LYS84 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 G 159 |
Chain | Residue |
E | GLU109 |
G | GLY46 |
G | SER47 |
G | GLY48 |
G | GLN49 |
G | LYS84 |
Functional Information from PROSITE/UniProt
site_id | PS01117 |
Number of Residues | 34 |
Details | HTH_MARR_1 MarR-type HTH domain signature. TA.Raiqk.LVdeGYVfrqrdekDRRsyrvflTekG |
Chain | Residue | Details |
A | THR78-GLY111 |