eF-site ID 1rk7_28-A
PDB Code 1rk7
Model 28
Chain A

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Title Solution structure of apo Cu,Zn Superoxide Dismutase: role of metal ions in protein folding
Classification OXIDOREDUCTASE
Compound Superoxide dismutase [Cu-Zn]
Source Homo sapiens (Human) (SODC_HUMAN)
Sequence A:  ATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE
GLHGFHVHEEEDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHSIIGRTLVVH
EKADDLGKGGNEQSTKTGNAGSRLACGVIGIAQ
Description


Functional site

1) chain A
residue 47
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

2) chain A
residue 49
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

3) chain A
residue 121
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

4) chain A
residue 64
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

5) chain A
residue 72
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

6) chain A
residue 81
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

7) chain A
residue 84
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

8) chain A
residue 4
type MOD_RES
sequence A
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

9) chain A
residue 10
type MOD_RES
sequence G
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

10) chain A
residue 92
type MOD_RES
sequence D
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

11) chain A
residue 2
type MOD_RES
sequence T
description N-acetylalanine => ECO:0000269|PubMed:1463506, ECO:0000269|PubMed:7002610, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI3

12) chain A
residue 99
type MOD_RES
sequence I
description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI5

13) chain A
residue 103
type MOD_RES
sequence V
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI6

14) chain A
residue 106
type MOD_RES
sequence L
description Phosphoserine => ECO:0000250|UniProtKB:P07632
source Swiss-Prot : SWS_FT_FI7

15) chain A
residue 108
type MOD_RES
sequence G
description Phosphoserine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI8

16) chain A
residue 123
type MOD_RES
sequence A
description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062
source Swiss-Prot : SWS_FT_FI9

17) chain A
residue 137
type MOD_RES
sequence T
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI10

18) chain A
residue 7
type LIPID
sequence V
description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122
source Swiss-Prot : SWS_FT_FI11

19) chain A
residue 33
type CROSSLNK
sequence G
description 1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33) => ECO:0000269|PubMed:20600836
source Swiss-Prot : SWS_FT_FI12

20) chain A
residue 138-149
type prosite
sequence GNAGSRLACGVI
description SOD_CU_ZN_2 Copper/Zinc superoxide dismutase signature 2. GNAGsRlACgvI
source prosite : PS00332


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