eF-site ID 6tiq_13-A
PDB Code 6tiq
Model 13
Chain A

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Title Refined solution NMR structure of hVDAC-1 in detergent micelles
Classification TRANSPORT PROTEIN
Compound Voltage-dependent anion-selective channel protein 1
Source (VDAC1_HUMAN)
Sequence A:  MAVPPTYADLGKSARDVFTKGYGFGLIKLDLKTKSENGLE
FTSSGSANTETTKVTGSLETKYRWTEYGLTFTEKWNTDNT
LGTEITVEDQLARGLKLTFDSSFSPNTGKKNAKIKTGYKR
EHINLGCDMDFDIAGPSIRGALVLGYEGWLAGYQMNFETA
KSRVTQSNFAVGYKTDEFQLHTNVNDGTEFGGSIYQKVNK
KLETAVNLAWTAGNSNTRFGIAAKYQIDPDACFSAKVNNS
SLIGLGYTQTLKPGIKLTLSALLDGKNVNAGGHKLGLGLE
FQALE
Description (1)  Voltage-dependent anion-selective channel protein 1


Functional site

1) chain A
residue 242
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:18755977
source Swiss-Prot : SWS_FT_FI2

2) chain A
residue 260
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:18755977
source Swiss-Prot : SWS_FT_FI2

3) chain A
residue 26-35
type TRANSMEM
sequence LIKLDLKTKS
description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158
source Swiss-Prot : SWS_FT_FI1

4) chain A
residue 150-158
type TRANSMEM
sequence LAGYQMNFE
description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158
source Swiss-Prot : SWS_FT_FI1

5) chain A
residue 163-175
type TRANSMEM
sequence RVTQSNFAVGYKT
description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158
source Swiss-Prot : SWS_FT_FI1

6) chain A
residue 178-185
type TRANSMEM
sequence FQLHTNVN
description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158
source Swiss-Prot : SWS_FT_FI1

7) chain A
residue 189-198
type TRANSMEM
sequence EFGGSIYQKV
description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158
source Swiss-Prot : SWS_FT_FI1

8) chain A
residue 202-211
type TRANSMEM
sequence LETAVNLAWT
description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158
source Swiss-Prot : SWS_FT_FI1

9) chain A
residue 218-227
type TRANSMEM
sequence RFGIAAKYQI
description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158
source Swiss-Prot : SWS_FT_FI1

10) chain A
residue 231-238
type TRANSMEM
sequence ACFSAKVN
description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158
source Swiss-Prot : SWS_FT_FI1

11) chain A
residue 242-251
type TRANSMEM
sequence LIGLGYTQTL
description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158
source Swiss-Prot : SWS_FT_FI1

12) chain A
residue 254-263
type TRANSMEM
sequence GIKLTLSALL
description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158
source Swiss-Prot : SWS_FT_FI1

13) chain A
residue 273-282
type TRANSMEM
sequence HKLGLGLEFQ
description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158
source Swiss-Prot : SWS_FT_FI1

14) chain A
residue 39-47
type TRANSMEM
sequence LEFTSSGSA
description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158
source Swiss-Prot : SWS_FT_FI1

15) chain A
residue 54-64
type TRANSMEM
sequence VTGSLETKYRW
description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158
source Swiss-Prot : SWS_FT_FI1

16) chain A
residue 69-76
type TRANSMEM
sequence LTFTEKWN
description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158
source Swiss-Prot : SWS_FT_FI1

17) chain A
residue 80-89
type TRANSMEM
sequence TLGTEITVED
description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158
source Swiss-Prot : SWS_FT_FI1

18) chain A
residue 95-104
type TRANSMEM
sequence LKLTFDSSFS
description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158
source Swiss-Prot : SWS_FT_FI1

19) chain A
residue 111-120
type TRANSMEM
sequence NAKIKTGYKR
description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158
source Swiss-Prot : SWS_FT_FI1

20) chain A
residue 123-130
type TRANSMEM
sequence INLGCDMD
description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158
source Swiss-Prot : SWS_FT_FI1

21) chain A
residue 137-145
type TRANSMEM
sequence SIRGALVLG
description Beta stranded => ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158
source Swiss-Prot : SWS_FT_FI1

22) chain A
residue 109
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:Q60932
source Swiss-Prot : SWS_FT_FI10

23) chain A
residue 193
type MOD_RES
sequence S
description Phosphoserine; by NEK1 => ECO:0000269|PubMed:20230784
source Swiss-Prot : SWS_FT_FI11

24) chain A
residue 225-247
type prosite
sequence YQIDPDACFSAKVNNSSLIGLGY
description EUKARYOTIC_PORIN Eukaryotic mitochondrial porin signature. YqiDPdAcfsAKVNNssliGLgY
source prosite : PS00558

25) chain A
residue 266
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI14

26) chain A
residue 12
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:32047033
source Swiss-Prot : SWS_FT_FI15

27) chain A
residue 53
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25621951, ECO:0000269|PubMed:32047033
source Swiss-Prot : SWS_FT_FI16

28) chain A
residue 110
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25621951, ECO:0000269|PubMed:32047033
source Swiss-Prot : SWS_FT_FI16

29) chain A
residue 274
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25621951, ECO:0000269|PubMed:32047033
source Swiss-Prot : SWS_FT_FI16

30) chain A
residue 20
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:32047033
source Swiss-Prot : SWS_FT_FI17

31) chain A
residue 61
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25621951
source Swiss-Prot : SWS_FT_FI18

32) chain A
residue 161
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25621951
source Swiss-Prot : SWS_FT_FI18

33) chain A
residue 109
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:25621951, ECO:0000269|PubMed:32047033
source Swiss-Prot : SWS_FT_FI19

34) chain A
residue 266
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:25621951
source Swiss-Prot : SWS_FT_FI20

35) chain A
residue 240
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI12

36) chain A
residue 252
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:Q60932
source Swiss-Prot : SWS_FT_FI13

37) chain A
residue 73
type SITE
sequence E
description Involved in ceramide and phosphatidylcholine binding. Critical for channel structural stability and gating => ECO:0000269|PubMed:31015432, ECO:0000305|PubMed:18832158
source Swiss-Prot : SWS_FT_FI3

38) chain A
residue 2
type MOD_RES
sequence A
description N-acetylalanine => ECO:0000269|PubMed:2559745, ECO:0000269|Ref.12, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI4

39) chain A
residue 13
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:Q9Z2L0
source Swiss-Prot : SWS_FT_FI5

40) chain A
residue 19
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:Q60932
source Swiss-Prot : SWS_FT_FI6

41) chain A
residue 20
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q60932
source Swiss-Prot : SWS_FT_FI7

42) chain A
residue 67
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q60932
source Swiss-Prot : SWS_FT_FI8

43) chain A
residue 107
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI9


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