eF-site ID 1wao-1
PDB Code 1wao
Chain 1

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Title PP5 structure
Classification HYDROLASE
Compound SERINE/THREONINE PROTEIN PHOSPHATASE 5
Source null (PPP5_HUMAN)
Sequence 1:  GALKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPSNA
IYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRR
AASNMALGKFRAALRDYETVVKVKPHDKDAKMKYQECNKI
VKQKAFERAKRSVVDSLDIESMTIEDEYSGPKLEDGKVTI
SFMKELMQWYKDQKKLHRKCAYQILVQVKEVLSKLSTLVE
TTLKETEKITVCGDTHGQFYDLLNIFELNGLPSETNPYIF
NGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDN
MNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKV
LIMHGGLFSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSD
PQPQNGRSISKRGVSCQFGPDVTKAFLEENNLDYIIRSHE
VKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSD
LRPQFHQFTAVPHPNVKPMAYANTLLQLGMM
Description (1)  SERINE/THREONINE PROTEIN PHOSPHATASE 5 (E.C.3.1.3.16)


Functional site

1) chain 1
residue 271
type
sequence D
description BINDING SITE FOR RESIDUE MN 1 601
source : AC1

2) chain 1
residue 303
type
sequence N
description BINDING SITE FOR RESIDUE MN 1 601
source : AC1

3) chain 1
residue 352
type
sequence H
description BINDING SITE FOR RESIDUE MN 1 601
source : AC1

4) chain 1
residue 427
type
sequence H
description BINDING SITE FOR RESIDUE MN 1 601
source : AC1

5) chain 1
residue 242
type
sequence D
description BINDING SITE FOR RESIDUE MN 1 602
source : AC2

6) chain 1
residue 244
type
sequence H
description BINDING SITE FOR RESIDUE MN 1 602
source : AC2

7) chain 1
residue 271
type
sequence D
description BINDING SITE FOR RESIDUE MN 1 602
source : AC2

8) chain 1
residue 451
type
sequence Y
description BINDING SITE FOR RESIDUE MN 1 602
source : AC2

9) chain 1
residue 304
type ACT_SITE
sequence H
description Proton donor/acceptor => ECO:0000269|PubMed:15155720
source Swiss-Prot : SWS_FT_FI1

10) chain 1
residue 300-305
type prosite
sequence LRGNHE
description SER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE
source prosite : PS00125

11) chain 1
residue 242
type catalytic
sequence D
description 472
source MCSA : MCSA1

12) chain 1
residue 244
type catalytic
sequence H
description 472
source MCSA : MCSA1

13) chain 1
residue 271
type catalytic
sequence D
description 472
source MCSA : MCSA1

14) chain 1
residue 274
type catalytic
sequence D
description 472
source MCSA : MCSA1

15) chain 1
residue 275
type catalytic
sequence R
description 472
source MCSA : MCSA1

16) chain 1
residue 303
type catalytic
sequence N
description 472
source MCSA : MCSA1

17) chain 1
residue 304
type catalytic
sequence H
description 472
source MCSA : MCSA1

18) chain 1
residue 352
type catalytic
sequence H
description 472
source MCSA : MCSA1

19) chain 1
residue 400
type catalytic
sequence R
description 472
source MCSA : MCSA1

20) chain 1
residue 427
type catalytic
sequence H
description 472
source MCSA : MCSA1

21) chain 1
residue 242
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:15155720, ECO:0000269|PubMed:15577939, ECO:0000269|PubMed:19601647, ECO:0007744|PDB:1S95, ECO:0007744|PDB:1WAO, ECO:0007744|PDB:3H60, ECO:0007744|PDB:3H61, ECO:0007744|PDB:3H62, ECO:0007744|PDB:3H63, ECO:0007744|PDB:3H64
source Swiss-Prot : SWS_FT_FI2

22) chain 1
residue 271
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:15155720, ECO:0000269|PubMed:15577939, ECO:0000269|PubMed:19601647, ECO:0007744|PDB:1S95, ECO:0007744|PDB:1WAO, ECO:0007744|PDB:3H60, ECO:0007744|PDB:3H61, ECO:0007744|PDB:3H62, ECO:0007744|PDB:3H63, ECO:0007744|PDB:3H64
source Swiss-Prot : SWS_FT_FI2

23) chain 1
residue 303
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:15155720, ECO:0000269|PubMed:15577939, ECO:0000269|PubMed:19601647, ECO:0007744|PDB:1S95, ECO:0007744|PDB:1WAO, ECO:0007744|PDB:3H60, ECO:0007744|PDB:3H61, ECO:0007744|PDB:3H62, ECO:0007744|PDB:3H63, ECO:0007744|PDB:3H64
source Swiss-Prot : SWS_FT_FI2

24) chain 1
residue 352
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:15155720, ECO:0000269|PubMed:15577939, ECO:0000269|PubMed:19601647, ECO:0007744|PDB:1S95, ECO:0007744|PDB:1WAO, ECO:0007744|PDB:3H60, ECO:0007744|PDB:3H61, ECO:0007744|PDB:3H62, ECO:0007744|PDB:3H63, ECO:0007744|PDB:3H64
source Swiss-Prot : SWS_FT_FI2

25) chain 1
residue 427
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:15155720
source Swiss-Prot : SWS_FT_FI3

26) chain 1
residue 244
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:15155720
source Swiss-Prot : SWS_FT_FI3

27) chain 1
residue 275
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:15155720
source Swiss-Prot : SWS_FT_FI3

28) chain 1
residue 400
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:15155720
source Swiss-Prot : SWS_FT_FI3


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