eF-site ID 6ag4-A
PDB Code 6ag4
Chain A

click to enlarge
Title Crystal structure of Ard1 N-terminal acetyltransferase H88A/E127A mutant from Sulfolobus solfataricus
Classification TRANSFERASE
Compound N-alpha-acetyltransferase
Source (NAT_SULSO)
Sequence A:  DFTLRNARMDDIDQIIKINRLTLPENYPYYFFVEHLKEYG
LAFFVAIVDNSVVGYIMPRIEWGFSNIKQLPSLVRKGAVV
SIAVLEEYRRKGIATTLLEASMKSMKNDYNAEEIYLAVRV
SNYPAIALYEKLNFKKVKVLKGYYADGEDAYLMARPL
Description


Functional site

1) chain A
residue 33
type
sequence L
description binding site for residue ACO A 201
source : AC1

2) chain A
residue 74
type
sequence F
description binding site for residue ACO A 201
source : AC1

3) chain A
residue 91
type
sequence S
description binding site for residue ACO A 201
source : AC1

4) chain A
residue 92
type
sequence I
description binding site for residue ACO A 201
source : AC1

5) chain A
residue 93
type
sequence A
description binding site for residue ACO A 201
source : AC1

6) chain A
residue 94
type
sequence V
description binding site for residue ACO A 201
source : AC1

7) chain A
residue 99
type
sequence R
description binding site for residue ACO A 201
source : AC1

8) chain A
residue 100
type
sequence R
description binding site for residue ACO A 201
source : AC1

9) chain A
residue 101
type
sequence K
description binding site for residue ACO A 201
source : AC1

10) chain A
residue 102
type
sequence G
description binding site for residue ACO A 201
source : AC1

11) chain A
residue 103
type
sequence I
description binding site for residue ACO A 201
source : AC1

12) chain A
residue 104
type
sequence A
description binding site for residue ACO A 201
source : AC1

13) chain A
residue 105
type
sequence T
description binding site for residue ACO A 201
source : AC1

14) chain A
residue 127
type
sequence A
description binding site for residue ACO A 201
source : AC1

15) chain A
residue 132
type
sequence N
description binding site for residue ACO A 201
source : AC1

16) chain A
residue 134
type
sequence P
description binding site for residue ACO A 201
source : AC1

17) chain A
residue 138
type
sequence L
description binding site for residue ACO A 201
source : AC1

18) chain A
residue 139
type
sequence Y
description binding site for residue ACO A 201
source : AC1

19) chain A
residue 141
type
sequence K
description binding site for residue ACO A 201
source : AC1

20) chain A
residue 61
type
sequence S
description binding site for residue SO4 A 202
source : AC2

21) chain A
residue 63
type
sequence V
description binding site for residue SO4 A 202
source : AC2

22) chain A
residue 72
type
sequence W
description binding site for residue SO4 A 202
source : AC2

23) chain A
residue 83
type
sequence L
description binding site for residue SO4 A 202
source : AC2

24) chain A
residue 95
type
sequence L
description binding site for residue SO4 A 202
source : AC2

25) chain A
residue 98
type
sequence Y
description binding site for residue SO4 A 202
source : AC2

26) chain A
residue 133
type
sequence Y
description binding site for residue SO4 A 202
source : AC2

27) chain A
residue 129
type
sequence R
description binding site for residue CA A 203
source : AC3

28) chain A
residue 132
type
sequence N
description binding site for residue CA A 203
source : AC3

29) chain A
residue 37
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:25728374, ECO:0007744|PDB:4R3L
source Swiss-Prot : SWS_FT_FI1

30) chain A
residue 154
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:25728374, ECO:0007744|PDB:4R3L
source Swiss-Prot : SWS_FT_FI1

31) chain A
residue 88
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:23959863, ECO:0007744|PDB:4LX9
source Swiss-Prot : SWS_FT_FI2

32) chain A
residue 127
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:23959863, ECO:0007744|PDB:4LX9
source Swiss-Prot : SWS_FT_FI2

33) chain A
residue 92
type BINDING
sequence I
description BINDING => ECO:0000269|PubMed:20419351, ECO:0000269|PubMed:23959863, ECO:0000269|PubMed:25728374, ECO:0000269|PubMed:26593285, ECO:0007744|PDB:2X7B, ECO:0007744|PDB:4LX9, ECO:0007744|PDB:4R3K, ECO:0007744|PDB:4R3L, ECO:0007744|PDB:5C88
source Swiss-Prot : SWS_FT_FI3

34) chain A
residue 100
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:20419351, ECO:0000269|PubMed:23959863, ECO:0000269|PubMed:25728374, ECO:0000269|PubMed:26593285, ECO:0007744|PDB:2X7B, ECO:0007744|PDB:4LX9, ECO:0007744|PDB:4R3K, ECO:0007744|PDB:4R3L, ECO:0007744|PDB:5C88
source Swiss-Prot : SWS_FT_FI3

35) chain A
residue 132
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:20419351, ECO:0000269|PubMed:23959863, ECO:0000269|PubMed:25728374, ECO:0007744|PDB:2X7B, ECO:0007744|PDB:4LX9, ECO:0007744|PDB:4R3K, ECO:0007744|PDB:4R3L
source Swiss-Prot : SWS_FT_FI4

36) chain A
residue 139
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:20419351, ECO:0000269|PubMed:23959863, ECO:0000269|PubMed:25728374, ECO:0007744|PDB:2X7B, ECO:0007744|PDB:4LX9, ECO:0007744|PDB:4R3K, ECO:0007744|PDB:4R3L
source Swiss-Prot : SWS_FT_FI4

37) chain A
residue 35
type SITE
sequence E
description Plays an important role in substrate specificity => ECO:0000269|PubMed:25728374
source Swiss-Prot : SWS_FT_FI5

38) chain A
residue 75
type SITE
sequence S
description Plays an important role in modulating multiple conformations of loop regions and contributes to protein thermostability => ECO:0000269|PubMed:26593285
source Swiss-Prot : SWS_FT_FI6

39) chain A
residue 82
type SITE
sequence S
description Plays an important role in modulating multiple conformations of loop regions and contributes to protein thermostability => ECO:0000269|PubMed:26593285
source Swiss-Prot : SWS_FT_FI6


Display surface

Download
Links