eF-site ID 5sxr-A
PDB Code 5sxr
Chain A

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Title Crystal structure of B. pseudomallei KatG with NAD bound
Classification OXIDOREDUCTASE
Compound Catalase-peroxidase
Source (KATG_BURP1)
Sequence A:  GTSNRDWWPNQLDLSILHRHSSLSDPMGKDFNYAQAFEKL
DLAAVKRDLHALMTTSQDWWPADFGHYGGLFIRMAXHSAG
TYRTADGRGGAGEGQQRFAPLNSWPDNANLDKARRLLWPI
KQKYGRAISWADLLILTGNVALESMGFKTFGFAGGRADTW
EPEDVYWGSEKIWLELSGGPNSRYSGDRQLENPLAAVQMG
LIYVNPEGPDGNPDPVAAARDIRDTFARMAMNDEETVALI
AGGHTFGKTHGAGPASNVGAEPEAAGIEAQGLGWKSAYRT
GKGADAITSGLEVTWTTTPTQWSHNFFENLFGYEWELTKS
PAGAHQWVAKGADAVIPDAFDPSKKHRPTMLTTDLSLRFD
PAYEKISRRFHENPEQFADAFARAWFKLTHRDMGPRARYL
GPEVPAEVLLWQDPIPAVDHPLIDAADAAELKAKVLASGL
TVSQLVSTAWAAASTFRGSDKRGGANGARIRLAPQKDWEA
NQPEQLAAVLETLEAIRTAFNGAQRGGKQVSLADLIVLAG
CAGVEQAAKNAGHAVTVPFAPGRADASQEQTDVESMAVLE
PVADGFRNYLKGKYRVPAEVLLVDKAQLLTLSAPEMTVLL
GGLRVLGANVGQSRHGVFTAREQALTNDFFVNLLDMGTEW
KPTAADADVFEGRDRATGELKWTGTRVDLVFGSHSQLRAL
AEVYGSADAQEKFVRDFVAVWNKVMNLDRFDLA
Description


Functional site

1) chain A
residue 104
type
sequence G
description binding site for residue HEM A 801
source : AC1

2) chain A
residue 105
type
sequence L
description binding site for residue HEM A 801
source : AC1

3) chain A
residue 111
type
sequence X
description binding site for residue HEM A 801
source : AC1

4) chain A
residue 239
type
sequence V
description binding site for residue HEM A 801
source : AC1

5) chain A
residue 274
type
sequence L
description binding site for residue HEM A 801
source : AC1

6) chain A
residue 278
type
sequence G
description binding site for residue HEM A 801
source : AC1

7) chain A
residue 279
type
sequence H
description binding site for residue HEM A 801
source : AC1

8) chain A
residue 282
type
sequence G
description binding site for residue HEM A 801
source : AC1

9) chain A
residue 283
type
sequence K
description binding site for residue HEM A 801
source : AC1

10) chain A
residue 284
type
sequence T
description binding site for residue HEM A 801
source : AC1

11) chain A
residue 285
type
sequence H
description binding site for residue HEM A 801
source : AC1

12) chain A
residue 323
type
sequence T
description binding site for residue HEM A 801
source : AC1

13) chain A
residue 324
type
sequence S
description binding site for residue HEM A 801
source : AC1

14) chain A
residue 388
type
sequence T
description binding site for residue HEM A 801
source : AC1

15) chain A
residue 420
type
sequence W
description binding site for residue HEM A 801
source : AC1

16) chain A
residue 122
type
sequence G
description binding site for residue NA A 802
source : AC2

17) chain A
residue 123
type
sequence R
description binding site for residue NA A 802
source : AC2

18) chain A
residue 124
type
sequence G
description binding site for residue NA A 802
source : AC2

19) chain A
residue 494
type
sequence S
description binding site for residue NA A 802
source : AC2

20) chain A
residue 124
type
sequence G
description binding site for residue CL A 803
source : AC3

21) chain A
residue 198
type
sequence E
description binding site for residue CL A 803
source : AC3

22) chain A
residue 200
type
sequence V
description binding site for residue CL A 803
source : AC3

23) chain A
residue 108
type
sequence R
description binding site for residue OXY A 804
source : AC4

24) chain A
residue 111
type
sequence X
description binding site for residue OXY A 804
source : AC4

25) chain A
residue 112
type
sequence H
description binding site for residue OXY A 804
source : AC4

26) chain A
residue 141
type
sequence D
description binding site for residue OXY A 804
source : AC4

27) chain A
residue 83
type
sequence D
description binding site for residue MPD A 805
source : AC5

28) chain A
residue 154
type
sequence P
description binding site for residue MPD A 805
source : AC5

29) chain A
residue 290
type
sequence A
description binding site for residue MRD A 806
source : AC6

30) chain A
residue 323
type
sequence T
description binding site for residue MRD A 806
source : AC6

31) chain A
residue 112
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01961
source Swiss-Prot : SWS_FT_FI1

32) chain A
residue 279
type BINDING
sequence H
description axial binding residue => ECO:0000255|HAMAP-Rule:MF_01961
source Swiss-Prot : SWS_FT_FI2

33) chain A
residue 108
type SITE
sequence R
description Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01961
source Swiss-Prot : SWS_FT_FI3

34) chain A
residue 111
type CROSSLNK
sequence X
description Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-244) => ECO:0000255|HAMAP-Rule:MF_01961
source Swiss-Prot : SWS_FT_FI4

35) chain A
residue 238
type CROSSLNK
sequence Y
description Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-91) => ECO:0000255|HAMAP-Rule:MF_01961
source Swiss-Prot : SWS_FT_FI5

36) chain A
residue 264
type CROSSLNK
sequence M
description Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-91) => ECO:0000255|HAMAP-Rule:MF_01961
source Swiss-Prot : SWS_FT_FI5

37) chain A
residue 271-281
type prosite
sequence TVALIAGGHTF
description PEROXIDASE_1 Peroxidases proximal heme-ligand signature. TVALIAGGHTF
source prosite : PS00435


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