eF-site ID 1n0j-AB
PDB Code 1n0j
Chain A, B

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Title The Structure of Human Mitochondrial MN3+ Superoxide Dismutase Reveals a Novel Tetrameric Interface of Two 4-Helix Bundles
Classification OXIDOREDUCTASE
Compound Superoxide dismutase [Mn]
Source Homo sapiens (Human) (SODM_HUMAN)
Sequence A:  KHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNV
TEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWTN
LSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQG
SGWGWLGFNKERGHLQIAACPNQDPLQGTTGLIPLLGIDV
WEHAYYLQYKNVRPDYLKAIWNVINWENVTERYMACKK
B:  KHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNV
TEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWTN
LSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQG
SGWGWLGFNKERGHLQIAACPNQDPLQGTTGLIPLLGIDV
WEHAYYLQYKNVRPDYLKAIWNVINWENVTERYMACKK
Description


Functional site

1) chain A
residue 26
type
sequence H
description active site, trigonal bipyramidal manganese
source : MNA

2) chain A
residue 74
type
sequence H
description active site, trigonal bipyramidal manganese
source : MNA

3) chain A
residue 159
type
sequence D
description active site, trigonal bipyramidal manganese
source : MNA

4) chain A
residue 163
type
sequence H
description active site, trigonal bipyramidal manganese
source : MNA

5) chain B
residue 26
type
sequence H
description active site, trigonal bipyramidal manganese
source : MNB

6) chain B
residue 74
type
sequence H
description active site, trigonal bipyramidal manganese
source : MNB

7) chain B
residue 159
type
sequence D
description active site, trigonal bipyramidal manganese
source : MNB

8) chain B
residue 163
type
sequence H
description active site, trigonal bipyramidal manganese
source : MNB

9) chain A
residue 26
type
sequence H
description BINDING SITE FOR RESIDUE MN A 199
source : AC1

10) chain A
residue 74
type
sequence H
description BINDING SITE FOR RESIDUE MN A 199
source : AC1

11) chain A
residue 159
type
sequence D
description BINDING SITE FOR RESIDUE MN A 199
source : AC1

12) chain A
residue 163
type
sequence H
description BINDING SITE FOR RESIDUE MN A 199
source : AC1

13) chain B
residue 26
type
sequence H
description BINDING SITE FOR RESIDUE MN B 199
source : AC2

14) chain B
residue 74
type
sequence H
description BINDING SITE FOR RESIDUE MN B 199
source : AC2

15) chain B
residue 159
type
sequence D
description BINDING SITE FOR RESIDUE MN B 199
source : AC2

16) chain B
residue 163
type
sequence H
description BINDING SITE FOR RESIDUE MN B 199
source : AC2

17) chain A
residue 159-166
type prosite
sequence DVWEHAYY
description SOD_MN Manganese and iron superoxide dismutases signature. DvWEHAYY
source prosite : PS00088

18) chain A
residue 26
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10852710, ECO:0000269|PubMed:11580280, ECO:0000269|PubMed:1394426, ECO:0000269|PubMed:19265433, ECO:0000269|PubMed:9537987, ECO:0000269|PubMed:9537988, ECO:0000312|PDB:1JA8, ECO:0007744|PDB:1AP5, ECO:0007744|PDB:1AP6, ECO:0007744|PDB:1EM1, ECO:0007744|PDB:1N0J, ECO:0007744|PDB:1QNM, ECO:0007744|PDB:1ZSP, ECO:0007744|PDB:1ZTE, ECO:0007744|PDB:1ZUQ, ECO:0007744|PDB:2P4K
source Swiss-Prot : SWS_FT_FI1

19) chain A
residue 74
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10852710, ECO:0000269|PubMed:11580280, ECO:0000269|PubMed:1394426, ECO:0000269|PubMed:19265433, ECO:0000269|PubMed:9537987, ECO:0000269|PubMed:9537988, ECO:0000312|PDB:1JA8, ECO:0007744|PDB:1AP5, ECO:0007744|PDB:1AP6, ECO:0007744|PDB:1EM1, ECO:0007744|PDB:1N0J, ECO:0007744|PDB:1QNM, ECO:0007744|PDB:1ZSP, ECO:0007744|PDB:1ZTE, ECO:0007744|PDB:1ZUQ, ECO:0007744|PDB:2P4K
source Swiss-Prot : SWS_FT_FI1

20) chain A
residue 159
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:10852710, ECO:0000269|PubMed:11580280, ECO:0000269|PubMed:1394426, ECO:0000269|PubMed:19265433, ECO:0000269|PubMed:9537987, ECO:0000269|PubMed:9537988, ECO:0000312|PDB:1JA8, ECO:0007744|PDB:1AP5, ECO:0007744|PDB:1AP6, ECO:0007744|PDB:1EM1, ECO:0007744|PDB:1N0J, ECO:0007744|PDB:1QNM, ECO:0007744|PDB:1ZSP, ECO:0007744|PDB:1ZTE, ECO:0007744|PDB:1ZUQ, ECO:0007744|PDB:2P4K
source Swiss-Prot : SWS_FT_FI1

21) chain A
residue 163
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10852710, ECO:0000269|PubMed:11580280, ECO:0000269|PubMed:1394426, ECO:0000269|PubMed:19265433, ECO:0000269|PubMed:9537987, ECO:0000269|PubMed:9537988, ECO:0000312|PDB:1JA8, ECO:0007744|PDB:1AP5, ECO:0007744|PDB:1AP6, ECO:0007744|PDB:1EM1, ECO:0007744|PDB:1N0J, ECO:0007744|PDB:1QNM, ECO:0007744|PDB:1ZSP, ECO:0007744|PDB:1ZTE, ECO:0007744|PDB:1ZUQ, ECO:0007744|PDB:2P4K
source Swiss-Prot : SWS_FT_FI1

22) chain B
residue 26
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10852710, ECO:0000269|PubMed:11580280, ECO:0000269|PubMed:1394426, ECO:0000269|PubMed:19265433, ECO:0000269|PubMed:9537987, ECO:0000269|PubMed:9537988, ECO:0000312|PDB:1JA8, ECO:0007744|PDB:1AP5, ECO:0007744|PDB:1AP6, ECO:0007744|PDB:1EM1, ECO:0007744|PDB:1N0J, ECO:0007744|PDB:1QNM, ECO:0007744|PDB:1ZSP, ECO:0007744|PDB:1ZTE, ECO:0007744|PDB:1ZUQ, ECO:0007744|PDB:2P4K
source Swiss-Prot : SWS_FT_FI1

23) chain B
residue 74
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10852710, ECO:0000269|PubMed:11580280, ECO:0000269|PubMed:1394426, ECO:0000269|PubMed:19265433, ECO:0000269|PubMed:9537987, ECO:0000269|PubMed:9537988, ECO:0000312|PDB:1JA8, ECO:0007744|PDB:1AP5, ECO:0007744|PDB:1AP6, ECO:0007744|PDB:1EM1, ECO:0007744|PDB:1N0J, ECO:0007744|PDB:1QNM, ECO:0007744|PDB:1ZSP, ECO:0007744|PDB:1ZTE, ECO:0007744|PDB:1ZUQ, ECO:0007744|PDB:2P4K
source Swiss-Prot : SWS_FT_FI1

24) chain B
residue 159
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:10852710, ECO:0000269|PubMed:11580280, ECO:0000269|PubMed:1394426, ECO:0000269|PubMed:19265433, ECO:0000269|PubMed:9537987, ECO:0000269|PubMed:9537988, ECO:0000312|PDB:1JA8, ECO:0007744|PDB:1AP5, ECO:0007744|PDB:1AP6, ECO:0007744|PDB:1EM1, ECO:0007744|PDB:1N0J, ECO:0007744|PDB:1QNM, ECO:0007744|PDB:1ZSP, ECO:0007744|PDB:1ZTE, ECO:0007744|PDB:1ZUQ, ECO:0007744|PDB:2P4K
source Swiss-Prot : SWS_FT_FI1

25) chain B
residue 163
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10852710, ECO:0000269|PubMed:11580280, ECO:0000269|PubMed:1394426, ECO:0000269|PubMed:19265433, ECO:0000269|PubMed:9537987, ECO:0000269|PubMed:9537988, ECO:0000312|PDB:1JA8, ECO:0007744|PDB:1AP5, ECO:0007744|PDB:1AP6, ECO:0007744|PDB:1EM1, ECO:0007744|PDB:1N0J, ECO:0007744|PDB:1QNM, ECO:0007744|PDB:1ZSP, ECO:0007744|PDB:1ZTE, ECO:0007744|PDB:1ZUQ, ECO:0007744|PDB:2P4K
source Swiss-Prot : SWS_FT_FI1

26) chain A
residue 34
type MOD_RES
sequence Y
description 3'-nitrotyrosine => ECO:0000269|PubMed:10334867, ECO:0000269|PubMed:16399855
source Swiss-Prot : SWS_FT_FI2

27) chain B
residue 34
type MOD_RES
sequence Y
description 3'-nitrotyrosine => ECO:0000269|PubMed:10334867, ECO:0000269|PubMed:16399855
source Swiss-Prot : SWS_FT_FI2

28) chain A
residue 44
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P09671
source Swiss-Prot : SWS_FT_FI3

29) chain A
residue 51
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P09671
source Swiss-Prot : SWS_FT_FI3

30) chain A
residue 98
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P09671
source Swiss-Prot : SWS_FT_FI3

31) chain A
residue 106
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P09671
source Swiss-Prot : SWS_FT_FI3

32) chain B
residue 44
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P09671
source Swiss-Prot : SWS_FT_FI3

33) chain B
residue 51
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P09671
source Swiss-Prot : SWS_FT_FI3

34) chain B
residue 98
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P09671
source Swiss-Prot : SWS_FT_FI3

35) chain B
residue 106
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P09671
source Swiss-Prot : SWS_FT_FI3

36) chain A
residue 90
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P09671
source Swiss-Prot : SWS_FT_FI4

37) chain A
residue 178
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P09671
source Swiss-Prot : SWS_FT_FI4

38) chain B
residue 90
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P09671
source Swiss-Prot : SWS_FT_FI4

39) chain B
residue 178
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P09671
source Swiss-Prot : SWS_FT_FI4


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