eF-site ID 1dgg-B
PDB Code 1dgg
Chain B

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Title HUMAN ERYTHROCYTE CATALSE CYANIDE COMPLEX
Classification OXIDOREDUCTASE
Compound CATALASE
Source ORGANISM_COMMON: human; ORGANISM_SCIENTIFIC: Homo sapiens;
Sequence B:  RDPASDQMQHWKEQRAAQKADVLTTGAGNPVGDKLNVITV
GPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGY
FEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGESGSAD
TVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSF
IHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDRG
IPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKN
LSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVM
TFNQAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPVN
YFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPDTHRH
RLGPNYLHIPVNCPYRARVANYQRDGPMCMQDNQGGAPNY
YPNSFGAPEQQPSALEHSIQYSGEVRRFNTANDDNVTQVR
AFYVNVLNEEQRKRLCENIAGHLKDAQIFIQKKAVKNFTE
VHPDYGSHIQALLDKYN
Description


Functional site

1) chain B
residue 74
type
sequence V
description BINDING SITE FOR RESIDUE CYN B 4001
source : AC2

2) chain B
residue 75
type
sequence H
description BINDING SITE FOR RESIDUE CYN B 4001
source : AC2

3) chain B
residue 161
type
sequence F
description BINDING SITE FOR RESIDUE CYN B 4001
source : AC2

4) chain B
residue 358
type
sequence Y
description BINDING SITE FOR RESIDUE CYN B 4001
source : AC2

5) chain B
residue 72
type
sequence R
description BINDING SITE FOR RESIDUE HEM B 2001
source : AC7

6) chain B
residue 74
type
sequence V
description BINDING SITE FOR RESIDUE HEM B 2001
source : AC7

7) chain B
residue 75
type
sequence H
description BINDING SITE FOR RESIDUE HEM B 2001
source : AC7

8) chain B
residue 112
type
sequence R
description BINDING SITE FOR RESIDUE HEM B 2001
source : AC7

9) chain B
residue 131
type
sequence G
description BINDING SITE FOR RESIDUE HEM B 2001
source : AC7

10) chain B
residue 146
type
sequence V
description BINDING SITE FOR RESIDUE HEM B 2001
source : AC7

11) chain B
residue 147
type
sequence G
description BINDING SITE FOR RESIDUE HEM B 2001
source : AC7

12) chain B
residue 148
type
sequence N
description BINDING SITE FOR RESIDUE HEM B 2001
source : AC7

13) chain B
residue 158
type
sequence P
description BINDING SITE FOR RESIDUE HEM B 2001
source : AC7

14) chain B
residue 161
type
sequence F
description BINDING SITE FOR RESIDUE HEM B 2001
source : AC7

15) chain B
residue 216
type
sequence G
description BINDING SITE FOR RESIDUE HEM B 2001
source : AC7

16) chain B
residue 217
type
sequence S
description BINDING SITE FOR RESIDUE HEM B 2001
source : AC7

17) chain B
residue 299
type
sequence L
description BINDING SITE FOR RESIDUE HEM B 2001
source : AC7

18) chain B
residue 334
type
sequence F
description BINDING SITE FOR RESIDUE HEM B 2001
source : AC7

19) chain B
residue 350
type
sequence M
description BINDING SITE FOR RESIDUE HEM B 2001
source : AC7

20) chain B
residue 354
type
sequence R
description BINDING SITE FOR RESIDUE HEM B 2001
source : AC7

21) chain B
residue 358
type
sequence Y
description BINDING SITE FOR RESIDUE HEM B 2001
source : AC7

22) chain B
residue 362
type
sequence H
description BINDING SITE FOR RESIDUE HEM B 2001
source : AC7

23) chain B
residue 365
type
sequence R
description BINDING SITE FOR RESIDUE HEM B 2001
source : AC7

24) chain B
residue 61
type
sequence M
description BINDING SITE FOR RESIDUE HEM D 2003
source : BC1

25) chain B
residue 65
type
sequence D
description BINDING SITE FOR RESIDUE HEM D 2003
source : BC1

26) chain B
residue 75
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000305|PubMed:10656833
source Swiss-Prot : SWS_FT_FI1

27) chain B
residue 148
type ACT_SITE
sequence N
description ACT_SITE => ECO:0000305|PubMed:10656833
source Swiss-Prot : SWS_FT_FI1

28) chain B
residue 417
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P24270
source Swiss-Prot : SWS_FT_FI10

29) chain B
residue 213
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:10656833, ECO:0007744|PDB:1DGB, ECO:0007744|PDB:1DGF, ECO:0007744|PDB:1DGG, ECO:0007744|PDB:1DGH
source Swiss-Prot : SWS_FT_FI2

30) chain B
residue 303
type BINDING
sequence W
description BINDING => ECO:0000269|PubMed:10656833, ECO:0007744|PDB:1DGB, ECO:0007744|PDB:1DGF, ECO:0007744|PDB:1DGG, ECO:0007744|PDB:1DGH
source Swiss-Prot : SWS_FT_FI2

31) chain B
residue 305
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10656833, ECO:0007744|PDB:1DGB, ECO:0007744|PDB:1DGF, ECO:0007744|PDB:1DGG, ECO:0007744|PDB:1DGH
source Swiss-Prot : SWS_FT_FI2

32) chain B
residue 194
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10656833, ECO:0007744|PDB:1DGB, ECO:0007744|PDB:1DGF, ECO:0007744|PDB:1DGG, ECO:0007744|PDB:1DGH
source Swiss-Prot : SWS_FT_FI2

33) chain B
residue 201
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:10656833, ECO:0007744|PDB:1DGB, ECO:0007744|PDB:1DGF, ECO:0007744|PDB:1DGG, ECO:0007744|PDB:1DGH
source Swiss-Prot : SWS_FT_FI2

34) chain B
residue 203
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:10656833, ECO:0007744|PDB:1DGB, ECO:0007744|PDB:1DGF, ECO:0007744|PDB:1DGG, ECO:0007744|PDB:1DGH
source Swiss-Prot : SWS_FT_FI2

35) chain B
residue 237
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:10656833, ECO:0007744|PDB:1DGB, ECO:0007744|PDB:1DGF, ECO:0007744|PDB:1DGH
source Swiss-Prot : SWS_FT_FI3

36) chain B
residue 306
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:10656833, ECO:0007744|PDB:1DGF
source Swiss-Prot : SWS_FT_FI4

37) chain B
residue 358
type BINDING
sequence Y
description axial binding residue => ECO:0000269|PubMed:10656833, ECO:0000269|PubMed:10666617, ECO:0007744|PDB:1DGB, ECO:0007744|PDB:1DGF, ECO:0007744|PDB:1DGG, ECO:0007744|PDB:1DGH, ECO:0007744|PDB:1F4J, ECO:0007744|PDB:1QQW
source Swiss-Prot : SWS_FT_FI5

38) chain B
residue 9
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI6

39) chain B
residue 422
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI6

40) chain B
residue 221
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:P24270
source Swiss-Prot : SWS_FT_FI7

41) chain B
residue 233
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P24270
source Swiss-Prot : SWS_FT_FI8

42) chain B
residue 499
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P24270
source Swiss-Prot : SWS_FT_FI8

43) chain B
residue 306
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270
source Swiss-Prot : SWS_FT_FI9

44) chain B
residue 480
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P24270
source Swiss-Prot : SWS_FT_FI9


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