eF-site ID 4rr0-ABC
PDB Code 4rr0
Chain A, B, C

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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


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