eF-site ID 4zfr-AB
PDB Code 4zfr
Chain A, B

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Title Catalytic domain of Sst2 F403A mutant bound to ubiquitin
Classification HYDROLASE
Compound AMSH-like protease sst2
Source (UBB_HUMAN)
Sequence A:  KIHAYTEGGKPLRTIYLPKLLKKVFLDVVKPNTKKNLETC
GILCGKLRQNAFFITHLVIPLQEATSDTCGTTDEASLFEF
QDKHNLLTLGWIHTHPTQTCFMSSVDLHTHCSYQLMLPEA
IAIVMAPSKNTSGIFRLLDPEGLQTIVKCRKPGLAHPHEG
KVYTMVAQPGHVREINSKLQVVDLR
B:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG
Description


Functional site

1) chain A
residue 356
type
sequence H
description binding site for residue ZN A 501
source : AC1

2) chain A
residue 397
type
sequence C
description binding site for residue ZN A 501
source : AC1

3) chain A
residue 404
type
sequence H
description binding site for residue ZN A 501
source : AC1

4) chain A
residue 406
type
sequence H
description binding site for residue ZN A 501
source : AC1

5) chain A
residue 341
type
sequence H
description binding site for residue ZN A 502
source : AC2

6) chain A
residue 343
type
sequence H
description binding site for residue ZN A 502
source : AC2

7) chain A
residue 354
type
sequence D
description binding site for residue ZN A 502
source : AC2

8) chain B
residue 76
type
sequence G
description binding site for residue ZN A 502
source : AC2

9) chain A
residue 381
type
sequence G
description binding site for residue EDO A 503
source : AC3

10) chain A
residue 382
type
sequence I
description binding site for residue EDO A 503
source : AC3

11) chain A
residue 413
type
sequence M
description binding site for residue EDO A 503
source : AC3

12) chain A
residue 414
type
sequence V
description binding site for residue EDO A 503
source : AC3

13) chain A
residue 416
type
sequence Q
description binding site for residue EDO A 503
source : AC3

14) chain B
residue 7
type
sequence T
description binding site for residue EDO B 101
source : AC4

15) chain B
residue 8
type
sequence L
description binding site for residue EDO B 101
source : AC4

16) chain B
residue 69
type
sequence L
description binding site for residue EDO B 101
source : AC4

17) chain B
residue 70
type
sequence V
description binding site for residue EDO B 101
source : AC4

18) chain B
residue 71
type
sequence L
description binding site for residue EDO B 101
source : AC4

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

20) chain A
residue 341
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01182
source Swiss-Prot : SWS_FT_FI1

21) chain A
residue 343
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01182
source Swiss-Prot : SWS_FT_FI1

22) chain A
residue 354
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU01182
source Swiss-Prot : SWS_FT_FI1

23) chain A
residue 356
type BINDING
sequence H
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

24) chain A
residue 397
type BINDING
sequence C
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

25) chain A
residue 404
type BINDING
sequence H
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

26) chain A
residue 406
type BINDING
sequence H
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

27) chain A
residue 286
type SITE
sequence E
description Indirect zinc-binding => ECO:0000250
source Swiss-Prot : SWS_FT_FI3


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