eF-site ID 2hd5-AB
PDB Code 2hd5
Chain A, B

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Title USP2 in complex with ubiquitin
Classification HYDROLASE
Compound Ubiquitin carboxyl-terminal hydrolase 2
Source ORGANISM_COMMON: cattle; ORGANISM_SCIENTIFIC: Bos taurus;
Sequence A:  QGLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRD
GSNAHTALVEEFAKLIQTIWTSSPNDVVSPSEFKTQIQRY
APRFVGYNQQDAQEFLRFLLDGLHNEVNRVHLPDDEKGRQ
MWRKYLEREDSRIGDLFVGQLKSSLTCTDCGYCSTVFDPF
WDLSLPIAVTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKR
CIKKFSIQRFPKILVLHLKRFSESRIRTSKLTTFVNFPLR
DLDLREFASENTNHAVYNLYAVSNHSGTTMGGHYTAYCRS
PGTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYELA
B:  MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQ
QRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG
Description


Functional site

1) chain A
residue 334
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 201
source : AC1

2) chain A
residue 337
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 201
source : AC1

3) chain A
residue 381
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 201
source : AC1

4) chain A
residue 384
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 201
source : AC1

5) chain B
residue 76
type MOD_RES
sequence G
description ADP-ribosylglycine => ECO:0000250|UniProtKB:P0CG48
source Swiss-Prot : SWS_FT_FI4

6) chain B
residue 6
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48
source Swiss-Prot : SWS_FT_FI5

7) chain B
residue 11
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48
source Swiss-Prot : SWS_FT_FI5

8) chain B
residue 27
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48
source Swiss-Prot : SWS_FT_FI5

9) chain B
residue 29
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48
source Swiss-Prot : SWS_FT_FI5

10) chain B
residue 33
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48
source Swiss-Prot : SWS_FT_FI5

11) chain B
residue 48
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48
source Swiss-Prot : SWS_FT_FI5

12) chain B
residue 63
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0CG48
source Swiss-Prot : SWS_FT_FI5

13) chain B
residue 76
type CROSSLNK
sequence G
description Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000255|PROSITE-ProRule:PRU00214
source Swiss-Prot : SWS_FT_FI6

14) chain A
residue 215-230
type prosite
sequence GLRNLGNTCFMNSILQ
description USP_1 Ubiquitin specific protease (USP) domain signature 1. GLrnlGNtCFMNSiLQ
source prosite : PS00972

15) chain A
residue 448-465
type prosite
sequence YNLYAVSNHSGTTMGGHY
description USP_2 Ubiquitin specific protease (USP) domain signature 2. YnLyAVsnHsGttmg..GHY
source prosite : PS00973

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

17) chain A
residue 223
type ACT_SITE
sequence C
description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093
source Swiss-Prot : SWS_FT_FI1

18) chain B
residue 72
type ACT_SITE
sequence R
description Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093
source Swiss-Prot : SWS_FT_FI1

19) chain A
residue 464
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093
source Swiss-Prot : SWS_FT_FI2

20) chain A
residue 334
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:16905103
source Swiss-Prot : SWS_FT_FI3

21) chain A
residue 337
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:16905103
source Swiss-Prot : SWS_FT_FI3

22) chain A
residue 381
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:16905103
source Swiss-Prot : SWS_FT_FI3

23) chain A
residue 384
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:16905103
source Swiss-Prot : SWS_FT_FI3


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