eF-site ID 6rkg-C
PDB Code 6rkg
Chain C

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Title 1.32 A RESOLUTION OF SPOROSARCINA PASTEURII UREASE INHIBITED IN THE PRESENCE OF NBPTO AT pH 7.5
Classification HYDROLASE
Compound Urease subunit gamma
Source ORGANISM_SCIENTIFIC: Sporosarcina pasteurii;
Sequence C:  MKINRQQYAESYGPTVGDQVRLADTDLWIEVEKDYTTYGD
EANFGGGKVLREGMGENGTYTRTENVLDLLLTNALILDYT
GIYKADIGVKDGYIVGIGKGGNPDIMDGVTPNMIVGTATE
VIAAEGKIVTAGGIDTHVHFINPDQVDVALANGITTLFGG
GTGPAEGSKATTVTPGPWNIEKMLKSTEGLPINVGILGKG
HGSSIAPIMEQIDAGAAGLXIHEDWGATPASIDRSLTVAD
EADVQVAIHSDTLNEAGFLEDTLRAINGRVIHSFHVEGAG
GGHAPDIMAMAGHPNVLPSSTNPTRPFTVNTIDEHLDMLM
VCHHLKQNIPEDVAFADSRIRPETIAAEDILHDLGIISMM
STDALAMGRAGEMVLRTWQTADKMKKQRGPLAEEKNGSDN
FRAKRYVSKYTINPAIAQGIAHEVGSIEEGKFADLVLWEP
KFFGVKADRVIKGGIIAYAQIGDPSASIPTPQPVMGRRMY
GTVGDLIHDTNITFMSKSSIQQGVPAKLGLKRRIGTVKNC
RNIGKKDMKWNDVTTDIDINPETYEVKVDGEVLTCEPVKE
LPMAQRYFLF
Description


Functional site

1) chain C
residue 309
type
sequence V
description binding site for residue EDO A 201
source : AC1

2) chain C
residue 310
type
sequence N
description binding site for residue EDO A 201
source : AC1

3) chain C
residue 559
type
sequence K
description binding site for residue EDO A 201
source : AC1

4) chain C
residue 568
type
sequence F
description binding site for residue EDO A 202
source : AC2

5) chain C
residue 570
type
sequence F
description binding site for residue EDO A 202
source : AC2

6) chain C
residue 229
type
sequence P
description binding site for residue EDO B 201
source : AC6

7) chain C
residue 220
type
sequence X
description binding site for residue NI C 601
source : AC8

8) chain C
residue 222
type
sequence H
description binding site for residue NI C 601
source : AC8

9) chain C
residue 249
type
sequence H
description binding site for residue NI C 601
source : AC8

10) chain C
residue 275
type
sequence H
description binding site for residue NI C 601
source : AC8

11) chain C
residue 280
type
sequence G
description binding site for residue NI C 601
source : AC8

12) chain C
residue 137
type
sequence H
description binding site for residue NI C 602
source : AC9

13) chain C
residue 139
type
sequence H
description binding site for residue NI C 602
source : AC9

14) chain C
residue 220
type
sequence X
description binding site for residue NI C 602
source : AC9

15) chain C
residue 363
type
sequence D
description binding site for residue NI C 602
source : AC9

16) chain C
residue 34
type
sequence D
description binding site for residue EDO C 603
source : AD1

17) chain C
residue 36
type
sequence T
description binding site for residue EDO C 603
source : AD1

18) chain C
residue 38
type
sequence Y
description binding site for residue EDO C 603
source : AD1

19) chain C
residue 7
type
sequence Q
description binding site for residue EDO C 604
source : AD2

20) chain C
residue 11
type
sequence S
description binding site for residue EDO C 604
source : AD2

21) chain C
residue 286
type
sequence D
description binding site for residue EDO C 605
source : AD3

22) chain C
residue 289
type
sequence A
description binding site for residue EDO C 605
source : AD3

23) chain C
residue 537
type
sequence I
description binding site for residue EDO C 605
source : AD3

24) chain C
residue 539
type
sequence I
description binding site for residue EDO C 605
source : AD3

25) chain C
residue 93
type
sequence Y
description binding site for residue EDO C 606
source : AD4

26) chain C
residue 423
type
sequence E
description binding site for residue EDO C 606
source : AD4

27) chain C
residue 501
type
sequence Q
description binding site for residue EDO C 606
source : AD4

28) chain C
residue 513
type
sequence R
description binding site for residue EDO C 606
source : AD4

29) chain C
residue 514
type
sequence I
description binding site for residue EDO C 606
source : AD4

30) chain C
residue 33
type
sequence K
description binding site for residue EDO C 607
source : AD5

31) chain C
residue 35
type
sequence Y
description binding site for residue EDO C 607
source : AD5

32) chain C
residue 536
type
sequence D
description binding site for residue EDO C 608
source : AD6

33) chain C
residue 538
type
sequence D
description binding site for residue EDO C 608
source : AD6

34) chain C
residue 547
type
sequence K
description binding site for residue EDO C 608
source : AD6

35) chain C
residue 549
type
sequence D
description binding site for residue EDO C 608
source : AD6

36) chain C
residue 550
type
sequence G
description binding site for residue EDO C 608
source : AD6

37) chain C
residue 337
type
sequence D
description binding site for residue EDO C 609
source : AD7

38) chain C
residue 338
type
sequence S
description binding site for residue EDO C 609
source : AD7

39) chain C
residue 544
type
sequence Y
description binding site for residue EDO C 609
source : AD7

40) chain C
residue 35
type
sequence Y
description binding site for residue EDO C 610
source : AD8

41) chain C
residue 83
type
sequence Y
description binding site for residue EDO C 610
source : AD8

42) chain C
residue 97
type
sequence I
description binding site for residue EDO C 610
source : AD8

43) chain C
residue 429
type
sequence E
description binding site for residue EDO C 610
source : AD8

44) chain C
residue 143
type
sequence P
description binding site for residue EDO C 611
source : AD9

45) chain C
residue 189
type
sequence G
description binding site for residue EDO C 611
source : AD9

46) chain C
residue 478
type
sequence R
description binding site for residue EDO C 611
source : AD9

47) chain C
residue 309
type
sequence V
description binding site for residue EDO C 612
source : AE1

48) chain C
residue 557
type
sequence P
description binding site for residue EDO C 612
source : AE1

49) chain C
residue 34
type
sequence D
description binding site for residue EDO C 613
source : AE2

50) chain C
residue 35
type
sequence Y
description binding site for residue EDO C 613
source : AE2

51) chain C
residue 317
type
sequence D
description binding site for residue EDO C 614
source : AE3

52) chain C
residue 327
type
sequence Q
description binding site for residue EDO C 614
source : AE3

53) chain C
residue 65
type
sequence N
description binding site for residue SO4 C 615
source : AE4

54) chain C
residue 204
type
sequence S
description binding site for residue SO4 C 615
source : AE4

55) chain C
residue 205
type
sequence I
description binding site for residue SO4 C 615
source : AE4

56) chain C
residue 558
type
sequence V
description binding site for residue SO4 C 616
source : AE5

57) chain C
residue 559
type
sequence K
description binding site for residue SO4 C 616
source : AE5

58) chain C
residue 560
type
sequence E
description binding site for residue SO4 C 616
source : AE5

59) chain C
residue 137
type
sequence H
description binding site for residue 2PA C 617
source : AE6

60) chain C
residue 139
type
sequence H
description binding site for residue 2PA C 617
source : AE6

61) chain C
residue 170
type
sequence A
description binding site for residue 2PA C 617
source : AE6

62) chain C
residue 220
type
sequence X
description binding site for residue 2PA C 617
source : AE6

63) chain C
residue 222
type
sequence H
description binding site for residue 2PA C 617
source : AE6

64) chain C
residue 249
type
sequence H
description binding site for residue 2PA C 617
source : AE6

65) chain C
residue 275
type
sequence H
description binding site for residue 2PA C 617
source : AE6

66) chain C
residue 280
type
sequence G
description binding site for residue 2PA C 617
source : AE6

67) chain C
residue 323
type
sequence H
description binding site for residue 2PA C 617
source : AE6

68) chain C
residue 363
type
sequence D
description binding site for residue 2PA C 617
source : AE6

69) chain C
residue 366
type
sequence A
description binding site for residue 2PA C 617
source : AE6

70) chain C
residue 367
type
sequence M
description binding site for residue 2PA C 617
source : AE6

71) chain C
residue 11
type
sequence S
description binding site for residue SO4 C 618
source : AE7

72) chain C
residue 12
type
sequence Y
description binding site for residue SO4 C 618
source : AE7

73) chain C
residue 43
type
sequence N
description binding site for residue SO4 C 618
source : AE7

74) chain C
residue 48
type
sequence K
description binding site for residue SO4 C 618
source : AE7

75) chain C
residue 326
type
sequence K
description binding site for residue SO4 C 618
source : AE7

76) chain C
residue 329
type
sequence I
description binding site for residue SO4 C 618
source : AE7

77) chain C
residue 511
type
sequence K
description binding site for residue SO4 C 619
source : AE8

78) chain C
residue 511
type
sequence K
description binding site for residue SO4 C 619
source : AE8

79) chain C
residue 511
type
sequence K
description binding site for residue SO4 C 619
source : AE8

80) chain C
residue 518
type
sequence K
description binding site for residue SO4 C 620
source : AE9

81) chain C
residue 518
type
sequence K
description binding site for residue SO4 C 620
source : AE9

82) chain C
residue 220
type MOD_RES
sequence X
description N6-carboxylysine => ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443, ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715, ECO:0000269|PubMed:30969470, ECO:0000269|DOI:10.1007/s007750050231, ECO:0007744|PDB:1IE7, ECO:0007744|PDB:1S3T, ECO:0007744|PDB:1UBP, ECO:0007744|PDB:2UBP, ECO:0007744|PDB:4UBP
source Swiss-Prot : SWS_FT_FI5

83) chain C
residue 323
type ACT_SITE
sequence H
description Proton donor => ECO:0000305
source Swiss-Prot : SWS_FT_FI1

84) chain C
residue 320-336
type prosite
sequence MVCHHLKQNIPEDVAFA
description UREASE_2 Urease active site. MVCHHLkqnIpeDVaFA
source prosite : PS00145

85) chain C
residue 130-143
type prosite
sequence TAGGIDTHVHFINP
description UREASE_1 Urease nickel ligands signature. TAGGIDtHVHfinP
source prosite : PS01120

86) chain C
residue 137
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443, ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715, ECO:0000269|PubMed:30969470, ECO:0000269|DOI:10.1007/s007750050231
source Swiss-Prot : SWS_FT_FI2

87) chain C
residue 275
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443, ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715, ECO:0000269|PubMed:30969470, ECO:0000269|DOI:10.1007/s007750050231
source Swiss-Prot : SWS_FT_FI2

88) chain C
residue 363
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443, ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715, ECO:0000269|PubMed:30969470, ECO:0000269|DOI:10.1007/s007750050231
source Swiss-Prot : SWS_FT_FI2

89) chain C
residue 139
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:30969470
source Swiss-Prot : SWS_FT_FI3

90) chain C
residue 170
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:30969470
source Swiss-Prot : SWS_FT_FI3

91) chain C
residue 222
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:30969470
source Swiss-Prot : SWS_FT_FI3

92) chain C
residue 249
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:30969470
source Swiss-Prot : SWS_FT_FI3

93) chain C
residue 366
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:30969470
source Swiss-Prot : SWS_FT_FI3

94) chain C
residue 220
type BINDING
sequence X
description via carbamate group => ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443, ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715, ECO:0000269|PubMed:30969470, ECO:0000269|DOI:10.1007/s007750050231
source Swiss-Prot : SWS_FT_FI4


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