Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003677 | molecular_function | DNA binding |
A | 0032784 | biological_process | regulation of DNA-templated transcription elongation |
A | 0046872 | molecular_function | metal ion binding |
A | 0070063 | molecular_function | RNA polymerase binding |
B | 0003677 | molecular_function | DNA binding |
B | 0032784 | biological_process | regulation of DNA-templated transcription elongation |
B | 0046872 | molecular_function | metal ion binding |
B | 0070063 | molecular_function | RNA polymerase binding |
C | 0003677 | molecular_function | DNA binding |
C | 0032784 | biological_process | regulation of DNA-templated transcription elongation |
C | 0046872 | molecular_function | metal ion binding |
C | 0070063 | molecular_function | RNA polymerase binding |
D | 0003677 | molecular_function | DNA binding |
D | 0032784 | biological_process | regulation of DNA-templated transcription elongation |
D | 0046872 | molecular_function | metal ion binding |
D | 0070063 | molecular_function | RNA polymerase binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 401 |
Chain | Residue |
A | GLU49 |
A | HOH426 |
A | HOH449 |
D | HIS132 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 402 |
Chain | Residue |
A | ASP63 |
A | GLU66 |
A | ZN416 |
B | ASP67 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN A 403 |
Chain | Residue |
A | HOH463 |
D | GLU24 |
A | GLU109 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 404 |
Chain | Residue |
A | GLU20 |
A | GLU24 |
A | HOH434 |
B | ALA2 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 405 |
Chain | Residue |
A | ZN413 |
B | ASP63 |
B | ZN414 |
B | HOH524 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN C 406 |
Chain | Residue |
A | ASP45 |
A | HOH439 |
C | ASP45 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 407 |
Chain | Residue |
B | ARG14 |
B | HIS132 |
C | GLU49 |
C | HOH510 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN C 408 |
Chain | Residue |
C | ARG23 |
C | GLU66 |
C | ZN423 |
C | HOH426 |
D | ASP67 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 409 |
Chain | Residue |
B | GLU24 |
B | GLN27 |
C | LEU85 |
C | GLU109 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN C 400 |
Chain | Residue |
A | ARG21 |
A | HOH499 |
C | GLU20 |
C | GLU24 |
D | ALA2 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 411 |
Chain | Residue |
C | MET1 |
C | ASP67 |
C | ZN421 |
D | ASP63 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN C 412 |
Chain | Residue |
C | HOH483 |
D | ASP114 |
D | LYS118 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 413 |
Chain | Residue |
A | ASP67 |
A | HOH425 |
B | ARG23 |
B | GLU66 |
B | ZN405 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN B 414 |
Chain | Residue |
B | ASP63 |
B | ZN405 |
B | HOH459 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN C 415 |
Chain | Residue |
C | ASP63 |
D | ASP63 |
D | ZN422 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 416 |
Chain | Residue |
A | ARG23 |
A | GLU66 |
A | ZN402 |
B | ASP67 |
B | ARG71 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 417 |
Chain | Residue |
A | ASP63 |
A | GLU66 |
B | ASP63 |
B | GLU66 |
site_id | BC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ZN D 418 |
site_id | CC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN A 419 |
Chain | Residue |
A | HIS132 |
A | ASP136 |
A | HOH483 |
site_id | CC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ZN B 420 |
Chain | Residue |
B | GLU54 |
B | HOH440 |
site_id | CC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN C 421 |
Chain | Residue |
C | ASP67 |
C | ZN411 |
D | ILE62 |
D | GLU66 |
D | HOH470 |
site_id | CC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN D 422 |
Chain | Residue |
C | ZN415 |
D | ASP63 |
D | HOH510 |
site_id | CC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ZN C 423 |
site_id | CC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ZN A 424 |
Chain | Residue |
A | PRO143 |
B | ASP114 |
site_id | CC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE ZN C 425 |
Functional Information from PROSITE/UniProt
site_id | PS00830 |
Number of Residues | 17 |
Details | GREAB_2 Prokaryotic transcription elongation factors signature 2. SdaSPMGkALLghrvGD |
Chain | Residue | Details |
A | SER120-ASP136 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | GLU20 | |
A | GLU24 | |
B | GLU20 | |
B | GLU24 | |
C | GLU20 | |
C | GLU24 | |
D | GLU20 | |
D | GLU24 | |