eF-site ID 3ihp-A
PDB Code 3ihp
Chain A

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Title Covalent Ubiquitin-Usp5 Complex
Classification HYDROLASE
Compound Ubiquitin carboxyl-terminal hydrolase 5
Source Homo sapiens (Human) (UBIQ_HUMAN)
Sequence A:  MAELSEEALLSVLPTIRVPKAGDRVHKDECAFSFDTPESE
GGLYICMNTFLGFGKQYVERHFNKTGQRVYLHLRRTDEDV
KIVILPDYLEIARDGLGGLPDIVRDRVTSAVEALLSVRQV
SKHAFSLKQLDNPARIPPCGWKCSKCDMRENLWLNLTDGS
ILCGRRYDGSGGNNHAVEHYRETGYPLAVKLGTITPDGAD
VYSYDEDDMVLDPSLAEHLSHFGIDMPLFGPGYTGIRNLG
NSCYLNSVVQVLFSIPDFQRKYVDKLEKIFQNAPTDPTQD
FSTQVAKLGHGLLSGEDGIAPRMFKALIGKGHPEFSTNRQ
QDAQEFFLHLINMVERNCRSSENPNEVFRFLVEEKIKCLA
TEKVKYTQRVDYIMQLPVPMDAALNKEELLEYEEKKRQAE
EEKMALPELVRAQVPFSSCLEAYGAPEQVDDFWSTALQAK
SVAVKTTRFASFPDYLVIQIKKFTFGLDWVPKKLDVSIEM
PEELDISQLRGTGLQPGEEELPDIESVIIQLVEMGFPMDA
CRKAVYYTGNSGAEAAMNWVMSHMDDPDFANPLILPPPED
CVTTIVSMGFSRDQALKALRATNNSLERAVDWIFSHIDDL
DAEAAMDPKVRDGPGKYQLFAFISHMGTSTMCGHYVCHIK
KEGRWVIYNDQKVCASEKPPKDLGYIYFYQRVA
Description


Functional site

1) chain A
residue 333
type
sequence N
description BINDING SITE FOR RESIDUE NEH C 76
source : AC1

2) chain A
residue 335
type
sequence C
description BINDING SITE FOR RESIDUE NEH C 76
source : AC1

3) chain A
residue 433
type
sequence Q
description BINDING SITE FOR RESIDUE NEH C 76
source : AC1

4) chain A
residue 794
type
sequence G
description BINDING SITE FOR RESIDUE NEH C 76
source : AC1

5) chain A
residue 199
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 836
source : AC4

6) chain A
residue 202
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 836
source : AC4

7) chain A
residue 219
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 836
source : AC4

8) chain A
residue 232
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 836
source : AC4

9) chain A
residue 327-342
type prosite
sequence GIRNLGNSCYLNSVVQ
description USP_1 Ubiquitin specific protease (USP) domain signature 1. GIrnlGNsCYLNSvVQ
source prosite : PS00972

10) chain A
residue 778-796
type prosite
sequence YQLFAFISHMGTSTMCGHY
description USP_2 Ubiquitin specific protease (USP) domain signature 2. YqLfAFisHmGtstmc.GHY
source prosite : PS00973

11) chain A
residue 175-283
type ZN_FING
sequence QVSKHAFSLKQLDNPARIPPCGWKCSKCDMRENLWLNLTD
GSILCGRRYDGSGGNNHAVEHYRETGYPLAVKLGTITPDG
ADVYSYDEDDMVLDPSLAEHLSHFGIDM
description UBP-type; degenerate => ECO:0000255|PROSITE-ProRule:PRU00502
source Swiss-Prot : SWS_FT_FI1

12) chain A
residue 779
type MOD_RES
sequence Q
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI10

13) chain A
residue 785
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI10

14) chain A
residue 783
type MOD_RES
sequence F
description Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI11

15) chain A
residue 335
type ACT_SITE
sequence C
description Nucleophile
source Swiss-Prot : SWS_FT_FI2

16) chain A
residue 818
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093
source Swiss-Prot : SWS_FT_FI3

17) chain A
residue 199
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00502
source Swiss-Prot : SWS_FT_FI4

18) chain A
residue 202
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00502
source Swiss-Prot : SWS_FT_FI4

19) chain A
residue 219
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00502
source Swiss-Prot : SWS_FT_FI4

20) chain A
residue 232
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00502
source Swiss-Prot : SWS_FT_FI4

21) chain A
residue 209
type BINDING
sequence W
description
source Swiss-Prot : SWS_FT_FI5

22) chain A
residue 221
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI5

23) chain A
residue 259
type BINDING
sequence Y
description
source Swiss-Prot : SWS_FT_FI5

24) chain A
residue 261
type BINDING
sequence Y
description
source Swiss-Prot : SWS_FT_FI5

25) chain A
residue 264
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI5

26) chain A
residue 2
type MOD_RES
sequence A
description N-acetylalanine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
source Swiss-Prot : SWS_FT_FI6

27) chain A
residue 156
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI7


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