eF-site ID 3a5w-ABCDEFGHIJ
PDB Code 3a5w
Chain A, B, C, D, E, F, G, H, I, J

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Title Peroxiredoxin (wild type) from Aeropyrum pernix K1 (reduced form)
Classification OXIDOREDUCTASE
Compound Probable peroxiredoxin
Source Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) (TDXH_AERPE)
Sequence A:  PGSIPLIGERFPEMEVTTDHGVIKLPDHYVSQGKWFVLFS
HPADFTPVCTTEFVSFARRYEDFQRLGVDLIGLSVDSVFS
HIKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHATHT
VRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKALKLG
DSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARMESGQ
YRCLDWWFCWDTPASRDDVEEARRYLRRAAEKPAKLLYEE
A
B:  PGSIPLIGERFPEMEVTTDHGVIKLPDHYVSQGKWFVLFS
HPADFTPVCTTEFVSFARRYEDFQRLGVDLIGLSVDSVFS
HIKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESA
THTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKAL
KLGDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARME
SGQYRCLDWWFCWDTPASRDDVEEARRYLRRAAEKPAKLL
YEEA
C:  PGSIPLIGERFPEMEVTTDHGVIKLPDHYVSQGKWFVLFS
HPADFTPVCTTEFVSFARRYEDFQRLGVDLIGLSVDSVFS
HIKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESA
THTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKAL
KLGDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARME
SGQYRCLDWWFCWDTPASRDDVEEARRYLRRAAEKPAKLL
YEEA
D:  PGSIPLIGERFPEMEVTTDHGVIKLPDHYVSQGKWFVLFS
HPADFTPVCTTEFVSFARRYEDFQRLGVDLIGLSVDSVFS
HIKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESA
THTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKAL
KLGDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARME
SGQYRCLDWWFCWDTPASRDDVEEARRYLRRAAEKPAKLL
YEEA
E:  PGSIPLIGERFPEMEVTTDHGVIKLPDHYVSQGKWFVLFS
HPADFTPVCTTEFVSFARRYEDFQRLGVDLIGLSVDSVFS
HIKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAATH
TVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKALKL
GDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARMESG
QYRCLDWWFCWDTPASRDDVEEARRYLRRAAEKPAKLLYE
EA
F:  PGSIPLIGERFPEMEVTTDHGVIKLPDHYVSQGKWFVLFS
HPADFTPVCTTEFVSFARRYEDFQRLGVDLIGLSVDSVFS
HIKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESA
THTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKAL
KLGDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARME
SGQYRCLDWWFCWDTPASRDDVEEARRYLRRAAEKPAKLL
YEEA
G:  PGSIPLIGERFPEMEVTTDHGVIKLPDHYVSQGKWFVLFS
HPADFTPVCTTEFVSFARRYEDFQRLGVDLIGLSVDSVFS
HIKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAATH
TVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKALKL
GDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARMESG
QYRCLDWWFCWDTPASRDDVEEARRYLRRAAEKPAKLLYE
EA
H:  PGSIPLIGERFPEMEVTTDHGVIKLPDHYVSQGKWFVLFS
HPADFTPVCTTEFVSFARRYEDFQRLGVDLIGLSVDSVFS
HIKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESA
THTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKAL
KLGDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARME
SGQYRCLDWWFCWDTPASRDDVEEARRYLRRAAEKPAKLL
YEE
I:  PGSIPLIGERFPEMEVTTDHGVIKLPDHYVSQGKWFVLFS
HPADFTPVCTTEFVSFARRYEDFQRLGVDLIGLSVDSVFS
HIKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAESA
THTVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKAL
KLGDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARME
SGQYRCLDWWFCWDTPASRDDVEEARRYLRRAAEKPAKLL
YEEA
J:  PGSIPLIGERFPEMEVTTDHGVIKLPDHYVSQGKWFVLFS
HPADFTPVCTTEFVSFARRYEDFQRLGVDLIGLSVDSVFS
HIKWKEWIERHIGVRIPFPIIADPQGTVARRLGLLHAATH
TVRGVFIVDARGVIRTMLYYPMELGRLVDEILRIVKALKL
GDSLKRAVPADWPNNEIIGEGLIVPPPTTEDQARARMESG
QYRCLDWWFCWDTPASRDDVEEARRYLRRAAEKPAKLLYE
E
Description (1)  Probable peroxiredoxin (E.C.1.11.1.15)


Functional site

1) chain A
residue 50
type ACT_SITE
sequence C
description Cysteine sulfenic acid (-SOH) intermediate => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:16214169, ECO:0000269|PubMed:18436649
source Swiss-Prot : SWS_FT_FI1

2) chain J
residue 50
type ACT_SITE
sequence C
description Cysteine sulfenic acid (-SOH) intermediate => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:16214169, ECO:0000269|PubMed:18436649
source Swiss-Prot : SWS_FT_FI1

3) chain B
residue 50
type ACT_SITE
sequence C
description Cysteine sulfenic acid (-SOH) intermediate => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:16214169, ECO:0000269|PubMed:18436649
source Swiss-Prot : SWS_FT_FI1

4) chain C
residue 50
type ACT_SITE
sequence C
description Cysteine sulfenic acid (-SOH) intermediate => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:16214169, ECO:0000269|PubMed:18436649
source Swiss-Prot : SWS_FT_FI1

5) chain D
residue 50
type ACT_SITE
sequence C
description Cysteine sulfenic acid (-SOH) intermediate => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:16214169, ECO:0000269|PubMed:18436649
source Swiss-Prot : SWS_FT_FI1

6) chain E
residue 50
type ACT_SITE
sequence C
description Cysteine sulfenic acid (-SOH) intermediate => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:16214169, ECO:0000269|PubMed:18436649
source Swiss-Prot : SWS_FT_FI1

7) chain F
residue 50
type ACT_SITE
sequence C
description Cysteine sulfenic acid (-SOH) intermediate => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:16214169, ECO:0000269|PubMed:18436649
source Swiss-Prot : SWS_FT_FI1

8) chain G
residue 50
type ACT_SITE
sequence C
description Cysteine sulfenic acid (-SOH) intermediate => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:16214169, ECO:0000269|PubMed:18436649
source Swiss-Prot : SWS_FT_FI1

9) chain H
residue 50
type ACT_SITE
sequence C
description Cysteine sulfenic acid (-SOH) intermediate => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:16214169, ECO:0000269|PubMed:18436649
source Swiss-Prot : SWS_FT_FI1

10) chain I
residue 50
type ACT_SITE
sequence C
description Cysteine sulfenic acid (-SOH) intermediate => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:16214169, ECO:0000269|PubMed:18436649
source Swiss-Prot : SWS_FT_FI1

11) chain A
residue 126
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:19819903
source Swiss-Prot : SWS_FT_FI2

12) chain J
residue 126
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:19819903
source Swiss-Prot : SWS_FT_FI2

13) chain B
residue 126
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:19819903
source Swiss-Prot : SWS_FT_FI2

14) chain C
residue 126
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:19819903
source Swiss-Prot : SWS_FT_FI2

15) chain D
residue 126
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:19819903
source Swiss-Prot : SWS_FT_FI2

16) chain E
residue 126
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:19819903
source Swiss-Prot : SWS_FT_FI2

17) chain F
residue 126
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:19819903
source Swiss-Prot : SWS_FT_FI2

18) chain G
residue 126
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:19819903
source Swiss-Prot : SWS_FT_FI2

19) chain H
residue 126
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:19819903
source Swiss-Prot : SWS_FT_FI2

20) chain I
residue 126
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00401, ECO:0000269|PubMed:19819903
source Swiss-Prot : SWS_FT_FI2


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