|
|
eF-site ID
|
6drd-L |
|
PDB Code
|
6drd |
|
Chain
|
L |
|
click to enlarge
|
|
|
Title
|
RNA Pol II(G) |
|
Classification
|
TRANSFERASE |
|
Compound
|
DNA-directed RNA polymerase II subunit RPB1 |
|
Source
|
ORGANISM_COMMON: Human; ORGANISM_SCIENTIFIC: Homo sapiens; |
|
|
Sequence
|
L: |
MIYICGECHTENEICRECGYRIMYKKRTKRLVVFDAR
|
|
|
Description
|
(1) |
DNA-directed RNA polymerase II subunit RPB1 (E.C.2.7.7.6,2.7.7.48), DNA-directed RNA polymerase II subunit RPB2 (E.C.2.7.7.6), DNA-directed RNA polymerase II subunit RPB3, DNA-directed RNA polymerase II subunit RPB4, DNA-directed RNA polymerases I, II, and III subunit RPABC1, DNA-directed RNA polymerases I, II, and III subunit RPABC2, DNA-directed RNA polymerase II subunit RPB7, DNA-directed RNA polymerases I, II, and III subunit RPABC3, DNA-directed RNA polymerase II subunit RPB9, DNA-directed RNA polymerases I, II, and III subunit RPABC5, DNA-directed RNA polymerase II subunit RPB11-a, DNA-directed RNA polymerases I, II, and III subunit RPABC4, Gdown1,DNA-directed RNA polymerase II subunit GRINL1A
|
|
Functional site
|
|
|
1)
|
chain |
L |
| residue |
19 |
| type |
|
| sequence |
C
|
| description |
binding site for residue ZN L 101
|
| source |
: AC5
|
|
|
2)
|
chain |
L |
| residue |
21 |
| type |
|
| sequence |
E
|
| description |
binding site for residue ZN L 101
|
| source |
: AC5
|
|
|
3)
|
chain |
L |
| residue |
22 |
| type |
|
| sequence |
C
|
| description |
binding site for residue ZN L 101
|
| source |
: AC5
|
|
|
4)
|
chain |
L |
| residue |
39 |
| type |
|
| sequence |
C
|
| description |
binding site for residue ZN L 101
|
| source |
: AC5
|
|
|
5)
|
chain |
L |
| residue |
22 |
| type |
BINDING |
| sequence |
C
|
| description |
BINDING => ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:33558764, ECO:0007744|PDB:5IY6, ECO:0007744|PDB:7AE1
|
| source |
Swiss-Prot : SWS_FT_FI3
|
|
|
6)
|
chain |
L |
| residue |
19-39 |
| type |
ZN_FING |
| sequence |
CGECHTENEICREC
|
| description |
C4-type => ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:33558766, ECO:0000269|PubMed:33674783, ECO:0000312|PDB:7DN3, ECO:0007744|PDB:7AE1, ECO:0007744|PDB:7D58
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
7)
|
chain |
L |
| residue |
19 |
| type |
BINDING |
| sequence |
C
|
| description |
BINDING => ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:33558766, ECO:0000269|PubMed:33674783, ECO:0000312|PDB:7DN3, ECO:0007744|PDB:5IY6, ECO:0007744|PDB:7AE1, ECO:0007744|PDB:7D58
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
8)
|
chain |
L |
| residue |
36 |
| type |
BINDING |
| sequence |
C
|
| description |
BINDING => ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:33558766, ECO:0007744|PDB:5IY6, ECO:0007744|PDB:7AE1, ECO:0007744|PDB:7D58
|
| source |
Swiss-Prot : SWS_FT_FI4
|
|
|
9)
|
chain |
L |
| residue |
39 |
| type |
BINDING |
| sequence |
C
|
| description |
BINDING => ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:33558766, ECO:0000269|PubMed:33674783, ECO:0000312|PDB:7DN3, ECO:0007744|PDB:5IY6, ECO:0007744|PDB:7D58
|
| source |
Swiss-Prot : SWS_FT_FI5
|
|
|
|