eF-site ID 5ofa-AB
PDB Code 5ofa
Chain A, B

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Title Crystal structure of human MORC2 (residues 1-603) with spinal muscular atrophy mutation T424R
Classification NUCLEAR PROTEIN
Compound MORC family CW-type zinc finger protein 2
Source (MORC2_HUMAN)
Sequence A:  TNYSSLNRAQLTFEYLHTNSTTHEFLFGALAELVDNARDA
DATRIDIYAERREDLRGGFMLCFLDDGAGMDPSDAASVIQ
FGKSAKRTPESTQIGQYGNGLKSGSMRIGKDFILFTKKED
TMTCLFLSRTFHEEEGIDEVIVPLPTWNARTREPVTDNVE
KFAIETELIYKYSPFRTEEEVMTQFMKIPGDSGTLVIIFN
LKLMDNGEPELDIISNPRDIQMAETKPERRSFRAYAAVLY
IDPRMRIFIHGHKVQTKRLSCCLYKPRMYKYTSSRFKTRA
EQEVKKAEHVARIAEEKAREAESKARTLEVRLGGDLTRDS
RVMLRQVQNRAITLRREADVKKRIKEAKQRALKEPKELNF
VFGVNIEHRDLDGMFIYNCSRLIKMYEKVGPQLEGGMACG
GVVGVVDVPYLVLEPRHNKQDFADAKEYRHLLRAMGEHLA
QYWKDIAIAQRGIIKFWDEFGYLSANWNQPPSSELRYKRR
RAMEIPTTIQCDLCLKWRTLPDTWVCSMNPDPEQDRCEAS
EQKQKVPLGTF
B:  NYSSLNRAQLTFEYLHTNSTTHEFLFGALAELVDNARDAD
ATRIDIYAERREDLRGGFMLCFLDDGAGMDPSDAASVIQF
GKSAKRTPESTQIGQYGNGLKSGSMRIGKDFILFTKKEDT
MTCLFLSRTFHEEEGIDEVIVPLPTWNARTREPVTDNVEK
FAIETELIYKYSPFRTEEEVMTQFMKIPGDSGTLVIIFNL
KLMDNGEPELDIISNPRDIQMAEEGTKPERRSFRAYAAVL
YIDPRMRIFIHGHKVQTKRLSCCLYKPRMYKYTSSRFKTR
AEQEVKKAEHVARIAEEKAREAESKARTLEVRLLTRDSRV
MLRQVQNRAITLRREADVKKRIKEAKQRALKEPKELNFVF
GVNIEHRDLDGMFIYNCSRLIKMYEKVGPQLEGGMACGGV
VGVVDVPYLVLEPRHNKQDFADAKEYRHLLRAMGEHLAQY
WKDIAIAQRGIIKFWDEFGYLSANWNQPPSSELRYKRRRA
MEIPTTIQCDLCLKWRTLPFQLSSVEKDYPDTWVCSMNPD
PEQDRCEASEQKQKVPLGTF
Description (1)  MORC family CW-type zinc finger protein 2


Functional site

1) chain B
residue 499
type
sequence C
description binding site for residue ZN B 701
source : AC1

2) chain B
residue 502
type
sequence C
description binding site for residue ZN B 701
source : AC1

3) chain B
residue 525
type
sequence C
description binding site for residue ZN B 701
source : AC1

4) chain B
residue 536
type
sequence C
description binding site for residue ZN B 701
source : AC1

5) chain B
residue 35
type
sequence E
description binding site for residue ANP B 702
source : AC2

6) chain B
residue 39
type
sequence N
description binding site for residue ANP B 702
source : AC2

7) chain B
residue 43
type
sequence A
description binding site for residue ANP B 702
source : AC2

8) chain B
residue 68
type
sequence D
description binding site for residue ANP B 702
source : AC2

9) chain B
residue 73
type
sequence M
description binding site for residue ANP B 702
source : AC2

10) chain B
residue 81
type
sequence V
description binding site for residue ANP B 702
source : AC2

11) chain B
residue 87
type
sequence S
description binding site for residue ANP B 702
source : AC2

12) chain B
residue 89
type
sequence K
description binding site for residue ANP B 702
source : AC2

13) chain B
residue 98
type
sequence G
description binding site for residue ANP B 702
source : AC2

14) chain B
residue 99
type
sequence Q
description binding site for residue ANP B 702
source : AC2

15) chain B
residue 100
type
sequence Y
description binding site for residue ANP B 702
source : AC2

16) chain B
residue 101
type
sequence G
description binding site for residue ANP B 702
source : AC2

17) chain B
residue 102
type
sequence N
description binding site for residue ANP B 702
source : AC2

18) chain B
residue 103
type
sequence G
description binding site for residue ANP B 702
source : AC2

19) chain B
residue 104
type
sequence L
description binding site for residue ANP B 702
source : AC2

20) chain B
residue 105
type
sequence K
description binding site for residue ANP B 702
source : AC2

21) chain B
residue 197
type
sequence T
description binding site for residue ANP B 702
source : AC2

22) chain B
residue 427
type
sequence K
description binding site for residue ANP B 702
source : AC2

23) chain B
residue 39
type
sequence N
description binding site for residue MG B 703
source : AC3

24) chain A
residue 499
type
sequence C
description binding site for residue ZN A 701
source : AC4

25) chain A
residue 502
type
sequence C
description binding site for residue ZN A 701
source : AC4

26) chain A
residue 525
type
sequence C
description binding site for residue ZN A 701
source : AC4

27) chain A
residue 536
type
sequence C
description binding site for residue ZN A 701
source : AC4

28) chain A
residue 35
type
sequence E
description binding site for residue ANP A 702
source : AC5

29) chain A
residue 39
type
sequence N
description binding site for residue ANP A 702
source : AC5

30) chain A
residue 43
type
sequence A
description binding site for residue ANP A 702
source : AC5

31) chain A
residue 68
type
sequence D
description binding site for residue ANP A 702
source : AC5

32) chain A
residue 73
type
sequence M
description binding site for residue ANP A 702
source : AC5

33) chain A
residue 81
type
sequence V
description binding site for residue ANP A 702
source : AC5

34) chain A
residue 87
type
sequence S
description binding site for residue ANP A 702
source : AC5

35) chain A
residue 89
type
sequence K
description binding site for residue ANP A 702
source : AC5

36) chain A
residue 98
type
sequence G
description binding site for residue ANP A 702
source : AC5

37) chain A
residue 99
type
sequence Q
description binding site for residue ANP A 702
source : AC5

38) chain A
residue 100
type
sequence Y
description binding site for residue ANP A 702
source : AC5

39) chain A
residue 101
type
sequence G
description binding site for residue ANP A 702
source : AC5

40) chain A
residue 102
type
sequence N
description binding site for residue ANP A 702
source : AC5

41) chain A
residue 103
type
sequence G
description binding site for residue ANP A 702
source : AC5

42) chain A
residue 104
type
sequence L
description binding site for residue ANP A 702
source : AC5

43) chain A
residue 105
type
sequence K
description binding site for residue ANP A 702
source : AC5

44) chain A
residue 197
type
sequence T
description binding site for residue ANP A 702
source : AC5

45) chain A
residue 427
type
sequence K
description binding site for residue ANP A 702
source : AC5

46) chain A
residue 39
type
sequence N
description binding site for residue MG A 703
source : AC6

47) chain B
residue 490-544
type ZN_FING
sequence AMEIPTTIQCDLCLKWRTLPFQLSSVEKDYPDTWVCSMNP
DPEQDRCEASEQKQK
description CW-type => ECO:0000255|PROSITE-ProRule:PRU00454, ECO:0000269|PubMed:29440755
source Swiss-Prot : SWS_FT_FI1

48) chain A
residue 490-544
type ZN_FING
sequence AMEIPTTIQCDLCLKWRTLPDTWVCSMNPDPEQDRCEASE
QKQK
description CW-type => ECO:0000255|PROSITE-ProRule:PRU00454, ECO:0000269|PubMed:29440755
source Swiss-Prot : SWS_FT_FI1

49) chain B
residue 39
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:29440755
source Swiss-Prot : SWS_FT_FI2

50) chain B
residue 87
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:29440755
source Swiss-Prot : SWS_FT_FI2

51) chain B
residue 99
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:29440755
source Swiss-Prot : SWS_FT_FI2

52) chain B
residue 427
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:29440755
source Swiss-Prot : SWS_FT_FI2

53) chain A
residue 39
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:29440755
source Swiss-Prot : SWS_FT_FI2

54) chain A
residue 87
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:29440755
source Swiss-Prot : SWS_FT_FI2

55) chain A
residue 99
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:29440755
source Swiss-Prot : SWS_FT_FI2

56) chain A
residue 427
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:29440755
source Swiss-Prot : SWS_FT_FI2

57) chain B
residue 499
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00454
source Swiss-Prot : SWS_FT_FI3

58) chain B
residue 502
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00454
source Swiss-Prot : SWS_FT_FI3

59) chain B
residue 525
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00454
source Swiss-Prot : SWS_FT_FI3

60) chain B
residue 536
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00454
source Swiss-Prot : SWS_FT_FI3

61) chain A
residue 499
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00454
source Swiss-Prot : SWS_FT_FI3

62) chain A
residue 502
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00454
source Swiss-Prot : SWS_FT_FI3

63) chain A
residue 525
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00454
source Swiss-Prot : SWS_FT_FI3

64) chain A
residue 536
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00454
source Swiss-Prot : SWS_FT_FI3


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