eF-site ID 6iih-AB
PDB Code 6iih
Chain A, B

click to enlarge
Title crystal structure of mitochondrial calcium uptake 2(MICU2)
Classification Calcium Binding Protein
Compound Endolysin,Calcium uptake protein 2, mitochondrial
Source (MICU2_HUMAN)
Sequence A:  MNIFEMLRIDERLRLKIYKDTEGYYTIGIGHLLTKSPSLN
AAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILR
NAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRM
LQQKRWDEAAVNLAKSIWYNQTPNRAKRVITTFRTGTWDA
YHMLRKQRFMQFSSLEHEGEYYMTPRDFLFSVMFEQMTSV
KKLTKKDIEDTLSGIQTAGCGSTFFRDLGDKGLISYTEYL
FLLTILTKPHSGFHVAFKMLDTDGNEMIEKREFFKLINTT
LQMRFFGKRGQRKLHYKEFRRFMENLQTEIQEMEFLQFSK
GLSFMRKEDFAEWLLFFTNTENKDIYWKNVREKLSAGESI
SLDEFKSFCHFTTHLEDFAIAMQMFSLAHRPVRLAEFKRA
VKVATGQELSNNILDTVFKIFDLDGDECLSHEEFLGVLKN
RMHRGL
B:  MNIFEMLRIDERLRLKIYKDTEGYYTIGIGHLLTKSPSLN
AAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILR
NAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRM
LQQKRWDEAAVNLAKSIWYNQTPNRAKRVITTFRTGTWDA
YHMLRKQRFMQFSSLEHEGEYYMTPRDFLFSVMFEQMEKK
LTKKDIEDTLSGIQTAGCGSTFFRDLGDKGLISYTEYLFL
LTILTKPHSGFHVAFKMLDTDGNEMIEKREFFKNTTLQMR
FFGKRGQRKLHYKEFRRFMENLQTEIQEMEFLQFSKGLSF
MRKEDFAEWLLFFTNTENKDIYWKNVREKLSAGESISLDE
FKSFCHFTTHLEDFAIAMQMFSLAHRPVRLAEFKRAVKVA
TGQELSNNILDTVFKIFDLDGDECLSHEEFLGVLKNR
Description


Functional site

1) chain A
residue 264
type
sequence D
description binding site for residue CA A 501
source : AC1

2) chain A
residue 266
type
sequence D
description binding site for residue CA A 501
source : AC1

3) chain A
residue 268
type
sequence N
description binding site for residue CA A 501
source : AC1

4) chain A
residue 270
type
sequence M
description binding site for residue CA A 501
source : AC1

5) chain A
residue 275
type
sequence E
description binding site for residue CA A 501
source : AC1

6) chain B
residue 264
type
sequence D
description binding site for residue CA B 501
source : AC2

7) chain B
residue 266
type
sequence D
description binding site for residue CA B 501
source : AC2

8) chain B
residue 268
type
sequence N
description binding site for residue CA B 501
source : AC2

9) chain B
residue 270
type
sequence M
description binding site for residue CA B 501
source : AC2

10) chain B
residue 272
type
sequence E
description binding site for residue CA B 501
source : AC2

11) chain B
residue 275
type
sequence E
description binding site for residue CA B 501
source : AC2

12) chain B
residue 454
type
sequence D
description binding site for residue CA B 502
source : AC3

13) chain B
residue 456
type
sequence D
description binding site for residue CA B 502
source : AC3

14) chain B
residue 458
type
sequence D
description binding site for residue CA B 502
source : AC3

15) chain B
residue 460
type
sequence C
description binding site for residue CA B 502
source : AC3

16) chain B
residue 465
type
sequence E
description binding site for residue CA B 502
source : AC3

17) chain A
residue 117
type BINDING
sequence S
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI4

18) chain A
residue 132
type BINDING
sequence N
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI4

19) chain B
residue 117
type BINDING
sequence S
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI4

20) chain B
residue 132
type BINDING
sequence N
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI4

21) chain A
residue 11
type catalytic
sequence E
description 921
source MCSA : MCSA1

22) chain A
residue 20
type catalytic
sequence D
description 921
source MCSA : MCSA1

23) chain B
residue 11
type catalytic
sequence E
description 921
source MCSA : MCSA2

24) chain B
residue 20
type catalytic
sequence D
description 921
source MCSA : MCSA2

25) chain A
residue 11
type ACT_SITE
sequence E
description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI1

26) chain B
residue 11
type ACT_SITE
sequence E
description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI1

27) chain A
residue 20
type ACT_SITE
sequence D
description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI2

28) chain B
residue 20
type ACT_SITE
sequence D
description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI2

29) chain B
residue 32
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI3

30) chain B
residue 104
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI3

31) chain A
residue 32
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI3

32) chain A
residue 104
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI3


Display surface

Download
Links