eF-site ID 1em1-A
PDB Code 1em1
Chain A

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Title X-RAY CRYSTAL STRUCTURE FOR HUMAN MANGANESE SUPEROXIDE DISMUTASE, Q143A
Classification OXIDOREDUCTASE
Compound MANGANESE SUPEROXIDE DISMUTASE
Source Homo sapiens (Human) (SODM_HUMAN)
Sequence A:  KHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNV
TEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWTN
LSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQG
SGWGWLGFNKERGHLQIAACPNADPLQGTTGLIPLLGIDV
WEHAYYLQYKNVRPDYLKAIWNVINWENVTERYMACKK
Description


Functional site

1) chain A
residue 178
type
sequence K
description BINDING SITE FOR RESIDUE SO4 B 500
source : AC1

2) chain A
residue 1
type
sequence K
description BINDING SITE FOR RESIDUE SO4 A 501
source : AC2

3) chain A
residue 2
type
sequence H
description BINDING SITE FOR RESIDUE SO4 A 501
source : AC2

4) chain A
residue 3
type
sequence S
description BINDING SITE FOR RESIDUE SO4 A 501
source : AC2

5) chain A
residue 71
type
sequence H
description BINDING SITE FOR RESIDUE SO4 A 501
source : AC2

6) chain A
residue 26
type
sequence H
description BINDING SITE FOR RESIDUE MN A 600
source : AC3

7) chain A
residue 74
type
sequence H
description BINDING SITE FOR RESIDUE MN A 600
source : AC3

8) chain A
residue 159
type
sequence D
description BINDING SITE FOR RESIDUE MN A 600
source : AC3

9) chain A
residue 163
type
sequence H
description BINDING SITE FOR RESIDUE MN A 600
source : AC3

10) 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

11) 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

12) 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

13) 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

14) 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

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

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

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

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

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

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

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


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