eF-site ID 3d6n-AB
PDB Code 3d6n
Chain A, B

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Title Crystal Structure of Aquifex Dihydroorotase Activated by Aspartate Transcarbamoylase
Classification HYDROLASE/TRANSFERASE
Compound Dihydroorotase
Source Aquifex aeolicus (PYRB_AQUAE)
Sequence A:  MLKLIVKNGYVIDPSQNLEGEFDILVENGKIKKIDKNILV
PEAEIIDAKGLIVCPGFIDIHVHLRDPGQTYKEDIESGSR
CAVAGGFTTIVCMPNTNPPIDNTTVVNYILQKSKSVGLCR
VLPTGTITKGRKGKEIADFYSLKEAGCVAFTDDGSPVMDS
SVMRKALELASQLGVPIMDHCEDDKLAYGVINEGEVSALL
GLSSRAPEAEEIQIARDGILAQRTGGHVHIQHVSTKLSLE
IIEFFKEKGVKITCEVNPNHLLFTEREVLNSGANARVNPP
LRKKEDRLALIEGVKRGIIDCFATDHAPHQTFEKELVEFA
MPGIIGLQTALPSALELYRKGIISLKKLIEMFTINPARII
GVDLGTLKLGSPADITIFDPNKEWILNEETNLSKSRNTPL
WGKVLKGKVIYTIKDGKMVYKD
B:  MRSLISSLDLTREEVEEILKYAKEFKEGKEETIKASAVLF
FSEPSTRTRLSFEKAARELGIETYLVSGSESSTVKGESFF
DTLKTFEGLGFDYVVFRVPFVFFPYKEIVKSLNLRLVNAG
DGTHQHPSQGLIDFFTIKEHFGEVKDLRVLYVGDIKHSRV
FRSGAPLLNMFGAKIGVCGPKTLIPRDVEVFKVDVFDDVD
KGIDWADVVIWLRLQKERQKENYIPSESSYFKQFGLTKER
FEKVKLYMHPGPVNRNVDIDHELVYTEKSLIQEQVKNGIP
VRKAIYKFLWT
Description


Functional site

1) chain A
residue 61
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 423
source : AC1

2) chain A
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 423
source : AC1

3) chain A
residue 153
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 423
source : AC1

4) chain A
residue 305
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 423
source : AC1

5) chain A
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE FLC A 424
source : AC2

6) chain A
residue 65
type
sequence R
description BINDING SITE FOR RESIDUE FLC A 424
source : AC2

7) chain A
residue 95
type
sequence N
description BINDING SITE FOR RESIDUE FLC A 424
source : AC2

8) chain A
residue 153
type
sequence D
description BINDING SITE FOR RESIDUE FLC A 424
source : AC2

9) chain A
residue 154
type
sequence G
description BINDING SITE FOR RESIDUE FLC A 424
source : AC2

10) chain A
residue 180
type
sequence H
description BINDING SITE FOR RESIDUE FLC A 424
source : AC2

11) chain A
residue 232
type
sequence H
description BINDING SITE FOR RESIDUE FLC A 424
source : AC2

12) chain A
residue 278
type
sequence N
description BINDING SITE FOR RESIDUE FLC A 424
source : AC2

13) chain A
residue 305
type
sequence D
description BINDING SITE FOR RESIDUE FLC A 424
source : AC2

14) chain A
residue 307
type
sequence A
description BINDING SITE FOR RESIDUE FLC A 424
source : AC2

15) chain A
residue 309
type
sequence H
description BINDING SITE FOR RESIDUE FLC A 424
source : AC2

16) chain A
residue 322
type
sequence P
description BINDING SITE FOR RESIDUE FLC A 424
source : AC2

17) chain A
residue 323
type
sequence G
description BINDING SITE FOR RESIDUE FLC A 424
source : AC2

18) chain B
residue 48
type
sequence T
description BINDING SITE FOR RESIDUE FLC B 292
source : AC3

19) chain B
residue 97
type
sequence R
description BINDING SITE FOR RESIDUE FLC B 292
source : AC3

20) chain B
residue 126
type
sequence H
description BINDING SITE FOR RESIDUE FLC B 292
source : AC3

21) chain B
residue 159
type
sequence R
description BINDING SITE FOR RESIDUE FLC B 292
source : AC3

22) chain B
residue 213
type
sequence R
description BINDING SITE FOR RESIDUE FLC B 292
source : AC3

23) chain B
residue 251
type
sequence G
description BINDING SITE FOR RESIDUE FLC B 292
source : AC3

24) chain B
residue 41-48
type prosite
sequence FSEPSTRT
description CARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FsEpSTRT
source prosite : PS00097

25) chain A
residue 59-67
type prosite
sequence DIHVHLRDP
description DIHYDROOROTASE_1 Dihydroorotase signature 1. DIHVHLRdP
source prosite : PS00482

26) chain A
residue 303-314
type prosite
sequence ATDHAPHQTFEK
description DIHYDROOROTASE_2 Dihydroorotase signature 2. ATDhAPHqtfeK
source prosite : PS00483

27) chain B
residue 47
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00001
source Swiss-Prot : SWS_FT_FI1

28) chain B
residue 252
type BINDING
sequence P
description BINDING => ECO:0000255|HAMAP-Rule:MF_00001
source Swiss-Prot : SWS_FT_FI1

29) chain B
residue 48
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_00001
source Swiss-Prot : SWS_FT_FI1

30) chain B
residue 75
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_00001
source Swiss-Prot : SWS_FT_FI1

31) chain B
residue 97
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00001
source Swiss-Prot : SWS_FT_FI1

32) chain B
residue 126
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_00001
source Swiss-Prot : SWS_FT_FI1

33) chain B
residue 129
type BINDING
sequence Q
description BINDING => ECO:0000255|HAMAP-Rule:MF_00001
source Swiss-Prot : SWS_FT_FI1

34) chain B
residue 159
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00001
source Swiss-Prot : SWS_FT_FI1

35) chain B
residue 213
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00001
source Swiss-Prot : SWS_FT_FI1

36) chain B
residue 251
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_00001
source Swiss-Prot : SWS_FT_FI1

37) chain A
residue 61
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:15826652, ECO:0000269|PubMed:19128030, ECO:0000269|PubMed:24314009, ECO:0007744|PDB:1XRF, ECO:0007744|PDB:1XRT, ECO:0007744|PDB:3D6N, ECO:0007744|PDB:4BJH
source Swiss-Prot : SWS_FT_FI2

38) chain A
residue 63
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:15826652, ECO:0000269|PubMed:19128030, ECO:0000269|PubMed:24314009, ECO:0007744|PDB:1XRF, ECO:0007744|PDB:1XRT, ECO:0007744|PDB:3D6N, ECO:0007744|PDB:4BJH
source Swiss-Prot : SWS_FT_FI2

39) chain A
residue 153
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:15826652, ECO:0000269|PubMed:19128030, ECO:0000269|PubMed:24314009, ECO:0007744|PDB:1XRF, ECO:0007744|PDB:1XRT, ECO:0007744|PDB:3D6N, ECO:0007744|PDB:4BJH
source Swiss-Prot : SWS_FT_FI2

40) chain A
residue 95
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_00220, ECO:0000305|PubMed:24314009, ECO:0007744|PDB:4BJH
source Swiss-Prot : SWS_FT_FI3

41) chain A
residue 278
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_00220, ECO:0000305|PubMed:24314009, ECO:0007744|PDB:4BJH
source Swiss-Prot : SWS_FT_FI3

42) chain A
residue 309
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_00220, ECO:0000305|PubMed:24314009, ECO:0007744|PDB:4BJH
source Swiss-Prot : SWS_FT_FI3

43) chain A
residue 322
type BINDING
sequence P
description BINDING => ECO:0000255|HAMAP-Rule:MF_00220, ECO:0000305|PubMed:24314009, ECO:0007744|PDB:4BJH
source Swiss-Prot : SWS_FT_FI3

44) chain A
residue 305
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:19128030, ECO:0000269|PubMed:24314009, ECO:0007744|PDB:3D6N, ECO:0007744|PDB:4BJH
source Swiss-Prot : SWS_FT_FI4


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