eF-site ID 4jzq-AB
PDB Code 4jzq
Chain A, B

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Title Crystal structure of human CLIC1 C24D mutant
Classification TRANSPORT PROTEIN
Compound Chloride intracellular channel protein 1
Source Homo sapiens (Human) (CLIC1_HUMAN)
Sequence A:  QPQVELFVKAGSDGAKIGNDPFSQRLFMVLWLKGVTFNVT
TVDTKRRTETVQKLCPGGQLPFLLYGTEVHTDTNKIEEFL
EAVLCPPRYPKLAALNPESNTAGLDIFAKFSAYIKNSNPA
LNDNLEKGLLKALKVLDNYLTSPLPEEVDETSAEDEGVSQ
RKFLDGNELTLADCNLLPKLHIVQVVCKKYRGFTIPEAFR
GVHRYLSNAYAREEFASTCPDDEEIELAYEQVAKALK
B:  QPQVELFVKAGSDGAKIGNDPFSQRLFMVLWLKGVTFNVT
TVDTKRRTETVQKLCPGGQLPFLLYGTEVHTDTNKIEEFL
EAVLCPPRYPKLAALNPESNTAGLDIFAKFSAYIKNSNPA
LNDNLEKGLLKALKVLDNYLTSPLPEEVDETSAEDEGVSQ
RKFLDGNELTLADCNLLPKLHIVQVVCKKYRGFTIPEAFR
GVHRYLSNAYAREEFASTCPDDEEIELAYEQVAK
Description


Functional site

1) chain A
residue 26-46
type TRANSMEM
sequence FSQRLFMVLWLKGVTFNVTTV
description Helical; Note=After insertion into the membrane => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

2) chain B
residue 26-46
type TRANSMEM
sequence FSQRLFMVLWLKGVTFNVTTV
description Helical; Note=After insertion into the membrane => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

3) chain A
residue 24
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:11551966, ECO:0007744|PDB:1K0N
source Swiss-Prot : SWS_FT_FI2

4) chain A
residue 64
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:11551966, ECO:0007744|PDB:1K0N
source Swiss-Prot : SWS_FT_FI2

5) chain A
residue 77
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:11551966, ECO:0007744|PDB:1K0N
source Swiss-Prot : SWS_FT_FI2

6) chain B
residue 24
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:11551966, ECO:0007744|PDB:1K0N
source Swiss-Prot : SWS_FT_FI2

7) chain B
residue 64
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:11551966, ECO:0007744|PDB:1K0N
source Swiss-Prot : SWS_FT_FI2

8) chain B
residue 77
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:11551966, ECO:0007744|PDB:1K0N
source Swiss-Prot : SWS_FT_FI2

9) chain A
residue 13
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

10) chain A
residue 119
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

11) chain A
residue 131
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

12) chain B
residue 13
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

13) chain B
residue 119
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

14) chain B
residue 131
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

15) chain A
residue 24
type MOD_RES
sequence D
description S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:14613939
source Swiss-Prot : SWS_FT_FI5

16) chain B
residue 24
type MOD_RES
sequence D
description S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:14613939
source Swiss-Prot : SWS_FT_FI5

17) chain A
residue 121
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI6

18) chain A
residue 156
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI6

19) chain A
residue 211
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI6

20) chain B
residue 121
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI6

21) chain B
residue 156
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI6

22) chain B
residue 211
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI6

23) chain A
residue 233
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q9Z1Q5
source Swiss-Prot : SWS_FT_FI7

24) chain B
residue 233
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q9Z1Q5
source Swiss-Prot : SWS_FT_FI7


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