eF-site ID 4pd4-E
PDB Code 4pd4
Chain E

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Title Structural analysis of atovaquone-inhibited cytochrome bc1 complex reveals the molecular basis of antimalarial drug action
Classification OXIDOREDUCTASE/INHIBITOR
Compound Cytochrome b-c1 complex subunit 1, mitochondrial
Source ORGANISM_COMMON: Baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae (strain ATCC 204508 / S288c);
Sequence E:  KSTYRTPNFDDVLKENNDADKGRSYAYFMVGAMGLLSSAG
AKSTVETFISSMTATADVLAMAKVEVNLAAIPLGKNVVVK
WQGKPVFIRHRTPHEIQEANSVDMSALKDPQTDADRVKDP
QWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGR
IRKGPAPLNLEIPAYEFDGDKVIVG
Description


Functional site

1) chain E
residue 57
type
sequence Y
description binding site for residue UMQ A 501
source : AC1

2) chain E
residue 68
type
sequence S
description binding site for residue UMQ A 501
source : AC1

3) chain E
residue 67
type
sequence S
description binding site for residue 3PH A 502
source : AC2

4) chain E
residue 181
type
sequence H
description binding site for residue AOQ C 4003
source : AC5

5) chain E
residue 159
type
sequence C
description binding site for residue FES E 301
source : AD1

6) chain E
residue 161
type
sequence H
description binding site for residue FES E 301
source : AD1

7) chain E
residue 162
type
sequence L
description binding site for residue FES E 301
source : AD1

8) chain E
residue 178
type
sequence C
description binding site for residue FES E 301
source : AD1

9) chain E
residue 180
type
sequence C
description binding site for residue FES E 301
source : AD1

10) chain E
residue 181
type
sequence H
description binding site for residue FES E 301
source : AD1

11) chain E
residue 183
type
sequence S
description binding site for residue FES E 301
source : AD1

12) chain E
residue 70
type
sequence G
description binding site for residue 3PH E 302
source : AD2

13) chain E
residue 71
type
sequence A
description binding site for residue 3PH E 302
source : AD2

14) chain E
residue 73
type
sequence S
description binding site for residue 3PH E 302
source : AD2

15) chain E
residue 74
type
sequence T
description binding site for residue 3PH E 302
source : AD2

16) chain E
residue 77
type
sequence T
description binding site for residue 3PH E 302
source : AD2

17) chain E
residue 178
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV, ECO:0007744|PDB:1KB9, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:1P84, ECO:0007744|PDB:2IBZ, ECO:0007744|PDB:3CX5, ECO:0007744|PDB:3CXH, ECO:0007744|PDB:4PD4
source Swiss-Prot : SWS_FT_FI4

18) chain E
residue 181
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV, ECO:0007744|PDB:1KB9, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:1P84, ECO:0007744|PDB:2IBZ, ECO:0007744|PDB:3CX5, ECO:0007744|PDB:3CXH, ECO:0007744|PDB:4PD4
source Swiss-Prot : SWS_FT_FI4

19) chain E
residue 159
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV, ECO:0007744|PDB:1KB9, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:1P84, ECO:0007744|PDB:2IBZ, ECO:0007744|PDB:3CX5, ECO:0007744|PDB:3CXH, ECO:0007744|PDB:4PD4
source Swiss-Prot : SWS_FT_FI4

20) chain E
residue 161
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV, ECO:0007744|PDB:1KB9, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:1P84, ECO:0007744|PDB:2IBZ, ECO:0007744|PDB:3CX5, ECO:0007744|PDB:3CXH, ECO:0007744|PDB:4PD4
source Swiss-Prot : SWS_FT_FI4

21) chain E
residue 181
type catalytic
sequence H
description 208
source MCSA : MCSA1


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