|
eF-site ID
|
4rr0-ABC |
PDB Code
|
4rr0 |
Chain
|
A, B, C |
|
click to enlarge
|
|
Title
|
re-refined 1vcw, CRYSTAL STRUCTURE OF DEGS AFTER BACKSOAKING THE ACTIVATING PEPTIDE |
Classification
|
HYDROLASE |
Compound
|
Protease degS |
Source
|
Escherichia coli P12b (H9UXC8_ECOLX) |
|
Sequence
|
A: |
MTPASYNLAVRRAAPAVVNVYNRGLNTNSHNQLEIRTLGS
GVIMDQRGYIITNKHVINDADQIIVALQDGRVFEALLVGS
DSLTDLAVLKINATGGLPTIPINARRVPHIGDVVLAIGNP
YNLGQTITQGIISATGRIGLNPTGRQNFLQTDASINHGNS
GGALVNSLGELMGINTLSETPEGIGFAIPFQLATKIMDKL
IRDGRVIRGYIGIVVNEVSPDGPAANAGIQVNDLIISVDN
KPAISALETMDQVAEIRPGSVIPVVVQLTLQVTIQEYPA
|
B: |
MTPASYNLAVRRAAPAVVNVYNEIRTLGSGVIMDQRGYII
TNKHVINDADQIIVALQDGRVFEALLVGSDSLTDLAVLKI
NATGGLPTIPINARRVPHIGDVVLAIGNPYNLGQTITQGI
ISATGRIGLNPTGRQNFLQTDASINHGNSGGALVNSLGEL
MGINTLTPEGIGFAIPFQLATKIMDKLIRDGRVIRGYIGI
GGRQGIVVNEVSPDGPAANAQVNDLIISVDNKPAISALET
MDQVAEIRPGSVIPVVVTLQVTIQEYPA
|
C: |
MTPASYNLAVRRAAPAVVNVYNRGLNTNNQLEIRTLGSGV
IMDQRGYIITNKHVINDADQIIVALQDGRVFEALLVGSDS
LTDLAVLKINATGGLPTIPINARRVPHIGDVVLAIGNPYN
LGQTITQGIISATGRIGLNPTGRQNFLQTDASINHGNSGG
ALVNSLGELMGINTLSETPEGIGFAIPFQLATKIMDKLIR
DGRVIRGYIGGIVVNEVSPDGPAANAGIQVNDLIISVDNK
PAISALETMDQVAEIRPGSVIPVVTIQEYPA
|
|
Description
|
|
Functional site
|
|
1)
|
chain |
C |
residue |
184 |
type |
BINDING |
sequence |
T
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
2)
|
chain |
C |
residue |
259 |
type |
BINDING |
sequence |
I
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
3)
|
chain |
C |
residue |
351 |
type |
BINDING |
sequence |
Y
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
4)
|
chain |
A |
residue |
184 |
type |
BINDING |
sequence |
T
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
5)
|
chain |
A |
residue |
259 |
type |
BINDING |
sequence |
I
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
6)
|
chain |
A |
residue |
351 |
type |
BINDING |
sequence |
Y
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
7)
|
chain |
B |
residue |
184 |
type |
BINDING |
sequence |
T
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
8)
|
chain |
B |
residue |
259 |
type |
BINDING |
sequence |
I
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
9)
|
chain |
B |
residue |
351 |
type |
BINDING |
sequence |
Y
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
10)
|
chain |
A |
residue |
96 |
type |
ACT_SITE |
sequence |
H
|
description |
Charge relay system => ECO:0000269|PubMed:15137941, ECO:0000269|PubMed:15225661, ECO:0000269|PubMed:20739286
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
11)
|
chain |
A |
residue |
126 |
type |
ACT_SITE |
sequence |
D
|
description |
Charge relay system => ECO:0000269|PubMed:15137941, ECO:0000269|PubMed:15225661, ECO:0000269|PubMed:20739286
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
12)
|
chain |
A |
residue |
201 |
type |
ACT_SITE |
sequence |
S
|
description |
Charge relay system => ECO:0000269|PubMed:15137941, ECO:0000269|PubMed:15225661, ECO:0000269|PubMed:20739286
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
13)
|
chain |
B |
residue |
96 |
type |
ACT_SITE |
sequence |
H
|
description |
Charge relay system => ECO:0000269|PubMed:15137941, ECO:0000269|PubMed:15225661, ECO:0000269|PubMed:20739286
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
14)
|
chain |
B |
residue |
126 |
type |
ACT_SITE |
sequence |
D
|
description |
Charge relay system => ECO:0000269|PubMed:15137941, ECO:0000269|PubMed:15225661, ECO:0000269|PubMed:20739286
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
15)
|
chain |
B |
residue |
201 |
type |
ACT_SITE |
sequence |
S
|
description |
Charge relay system => ECO:0000269|PubMed:15137941, ECO:0000269|PubMed:15225661, ECO:0000269|PubMed:20739286
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
16)
|
chain |
C |
residue |
96 |
type |
ACT_SITE |
sequence |
H
|
description |
Charge relay system => ECO:0000269|PubMed:15137941, ECO:0000269|PubMed:15225661, ECO:0000269|PubMed:20739286
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
17)
|
chain |
C |
residue |
126 |
type |
ACT_SITE |
sequence |
D
|
description |
Charge relay system => ECO:0000269|PubMed:15137941, ECO:0000269|PubMed:15225661, ECO:0000269|PubMed:20739286
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
18)
|
chain |
C |
residue |
201 |
type |
ACT_SITE |
sequence |
S
|
description |
Charge relay system => ECO:0000269|PubMed:15137941, ECO:0000269|PubMed:15225661, ECO:0000269|PubMed:20739286
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
|
|