eF-site ID 1b3o-B
PDB Code 1b3o
Chain B

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Title TERNARY COMPLEX OF HUMAN TYPE-II INOSINE MONOPHOSPHATE DEHYDROGENASE WITH 6-CL-IMP AND SELENAZOLE ADENINE DINUCLEOTIDE
Classification DEHYDROGENASE
Compound PROTEIN (INOSINE MONOPHOSPHATE DEHYDROGENASE 2)
Source Homo sapiens (Human) (IMDH2_HUMAN)
Sequence B:  TSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQV
DLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIG
FIHHNCTPEFQANEVRKVKKYEQGFITDPVVLSPKDRVRD
CGIPITDTGRMGSRLVGIISIMTKREDLVVAPAGITLKEA
NEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLAS
KDAKKQLLCGAAIGTHEDDKYRLDLLAQAGVDVVVLDSSQ
GNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAG
VDALRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRF
GVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAP
GEYDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRAMMYS
GELKFEKRTSSAQV
Description


Functional site

1) chain B
residue 68
type
sequence S
description BINDING SITE FOR RESIDUE CPR B 631
source : AC2

2) chain B
residue 322
type
sequence R
description BINDING SITE FOR RESIDUE CPR B 631
source : AC2

3) chain B
residue 328
type
sequence G
description BINDING SITE FOR RESIDUE CPR B 631
source : AC2

4) chain B
residue 329
type
sequence S
description BINDING SITE FOR RESIDUE CPR B 631
source : AC2

5) chain B
residue 331
type
sequence C
description BINDING SITE FOR RESIDUE CPR B 631
source : AC2

6) chain B
residue 334
type
sequence Q
description BINDING SITE FOR RESIDUE CPR B 631
source : AC2

7) chain B
residue 335
type
sequence E
description BINDING SITE FOR RESIDUE CPR B 631
source : AC2

8) chain B
residue 364
type
sequence D
description BINDING SITE FOR RESIDUE CPR B 631
source : AC2

9) chain B
residue 365
type
sequence G
description BINDING SITE FOR RESIDUE CPR B 631
source : AC2

10) chain B
residue 366
type
sequence G
description BINDING SITE FOR RESIDUE CPR B 631
source : AC2

11) chain B
residue 387
type
sequence G
description BINDING SITE FOR RESIDUE CPR B 631
source : AC2

12) chain B
residue 388
type
sequence S
description BINDING SITE FOR RESIDUE CPR B 631
source : AC2

13) chain B
residue 45
type
sequence T
description BINDING SITE FOR RESIDUE SAE B 601
source : AC4

14) chain B
residue 252
type
sequence T
description BINDING SITE FOR RESIDUE SAE B 601
source : AC4

15) chain B
residue 253
type
sequence H
description BINDING SITE FOR RESIDUE SAE B 601
source : AC4

16) chain B
residue 274
type
sequence D
description BINDING SITE FOR RESIDUE SAE B 601
source : AC4

17) chain B
residue 275
type
sequence S
description BINDING SITE FOR RESIDUE SAE B 601
source : AC4

18) chain B
residue 276
type
sequence S
description BINDING SITE FOR RESIDUE SAE B 601
source : AC4

19) chain B
residue 282
type
sequence F
description BINDING SITE FOR RESIDUE SAE B 601
source : AC4

20) chain B
residue 303
type
sequence N
description BINDING SITE FOR RESIDUE SAE B 601
source : AC4

21) chain B
residue 324
type
sequence G
description BINDING SITE FOR RESIDUE SAE B 601
source : AC4

22) chain B
residue 334
type
sequence Q
description BINDING SITE FOR RESIDUE SAE B 601
source : AC4

23) chain B
residue 466
type
sequence H
description BINDING SITE FOR RESIDUE SAE B 601
source : AC4

24) chain B
residue 469
type
sequence Q
description BINDING SITE FOR RESIDUE SAE B 601
source : AC4

25) chain B
residue 331
type ACT_SITE
sequence C
description Thioimidate intermediate => ECO:0000255|HAMAP-Rule:MF_03156, ECO:0000269|PubMed:10097070
source Swiss-Prot : SWS_FT_FI1

26) chain B
residue 195
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI11

27) chain B
residue 208
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI11

28) chain B
residue 274
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI3

29) chain B
residue 364
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI3

30) chain B
residue 387
type BINDING
sequence G
description
source Swiss-Prot : SWS_FT_FI3

31) chain B
residue 324
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_03156
source Swiss-Prot : SWS_FT_FI4

32) chain B
residue 329
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_03156
source Swiss-Prot : SWS_FT_FI4

33) chain B
residue 326
type BINDING
sequence G
description in other chain => ECO:0000255|HAMAP-Rule:MF_03156, ECO:0000269|Ref.28
source Swiss-Prot : SWS_FT_FI5

34) chain B
residue 328
type BINDING
sequence G
description in other chain => ECO:0000255|HAMAP-Rule:MF_03156, ECO:0000269|Ref.28
source Swiss-Prot : SWS_FT_FI5

35) chain B
residue 331
type BINDING
sequence C
description in other chain => ECO:0000255|HAMAP-Rule:MF_03156, ECO:0000269|Ref.28
source Swiss-Prot : SWS_FT_FI5

36) chain B
residue 122
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI6

37) chain B
residue 400
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:15592455
source Swiss-Prot : SWS_FT_FI8


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