eF-site ID 3prm-ABCD
PDB Code 3prm
Chain A, B, C, D

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Title Structural analysis of a viral OTU domain protease from the Crimean-Congo Hemorrhagic Fever virus in complex with human ubiquitin
Classification HYDROLASE/HYDROLASE
Compound RNA-directed RNA polymerase L
Source Homo sapiens (Human) (J3QS39_HUMAN)
Sequence A:  DFLRSLDWTQVIAGQYVSNPRFNISDYFEIVRQPGDGNCF
YHSIAELTXPNKTDHSYHYIKRLTESAARKYYQEEPEARL
VGLSLEDYLKRXLSDNEWGSTLEASXLAKEXGITIIIWTV
AASDEVEAGIKFGDGDVFTAVNLLHSGQTHFDALRILPQF
E
B:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGX
C:  DFLRSLDWTQVIAGQYVSNPRFNISDYFEIVRQPGDGNCF
YHSIAELTXPNKTDHSYHYIKRLTESAARKYYQEEPEARL
VGLSLEDYLKRXLSDNEWGSTLEASXLAKEXGITIIIWTV
AASDEVEAGIKFGDGDVFTAVNLLHSGQTHFDALRILPQF
E
D:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGX
Description


Functional site

1) chain A
residue 38
type
sequence G
description BINDING SITE FOR RESIDUE 4LJ B 76
source : AC1

2) chain A
residue 40
type
sequence C
description BINDING SITE FOR RESIDUE 4LJ B 76
source : AC1

3) chain A
residue 99
type
sequence W
description BINDING SITE FOR RESIDUE 4LJ B 76
source : AC1

4) chain A
residue 150
type
sequence T
description BINDING SITE FOR RESIDUE 4LJ B 76
source : AC1

5) chain A
residue 151
type
sequence H
description BINDING SITE FOR RESIDUE 4LJ B 76
source : AC1

6) chain B
residue 48
type
sequence K
description BINDING SITE FOR RESIDUE 4LJ B 76
source : AC1

7) chain B
residue 75
type
sequence G
description BINDING SITE FOR RESIDUE 4LJ B 76
source : AC1

8) chain C
residue 40
type
sequence C
description BINDING SITE FOR RESIDUE 4LJ D 76
source : AC2

9) chain C
residue 99
type
sequence W
description BINDING SITE FOR RESIDUE 4LJ D 76
source : AC2

10) chain C
residue 150
type
sequence T
description BINDING SITE FOR RESIDUE 4LJ D 76
source : AC2

11) chain D
residue 75
type
sequence G
description BINDING SITE FOR RESIDUE 4LJ D 76
source : AC2

12) chain B
residue 27-52
type prosite
sequence KAKIQDKEGIPPDQQRLIFAGKQLED
description UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
source prosite : PS00299

13) chain A
residue 40
type ACT_SITE
sequence C
description For ubiquitin thioesterase activity => ECO:0000269|PubMed:21228232, ECO:0000269|PubMed:21266548
source Swiss-Prot : SWS_FT_FI1

14) chain A
residue 153
type ACT_SITE
sequence D
description For ubiquitin thioesterase activity => ECO:0000269|PubMed:21228232, ECO:0000269|PubMed:21266548
source Swiss-Prot : SWS_FT_FI1

15) chain C
residue 40
type ACT_SITE
sequence C
description For ubiquitin thioesterase activity => ECO:0000269|PubMed:21228232, ECO:0000269|PubMed:21266548
source Swiss-Prot : SWS_FT_FI1

16) chain C
residue 153
type ACT_SITE
sequence D
description For ubiquitin thioesterase activity => ECO:0000269|PubMed:21228232, ECO:0000269|PubMed:21266548
source Swiss-Prot : SWS_FT_FI1

17) chain A
residue 151
type ACT_SITE
sequence H
description For ubiquitin thioesterase activity => ECO:0000269|PubMed:21228232, ECO:0000269|PubMed:21266548, ECO:0000305|PubMed:18078692
source Swiss-Prot : SWS_FT_FI2

18) chain C
residue 151
type ACT_SITE
sequence H
description For ubiquitin thioesterase activity => ECO:0000269|PubMed:21228232, ECO:0000269|PubMed:21266548, ECO:0000305|PubMed:18078692
source Swiss-Prot : SWS_FT_FI2


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