eF-site ID 1ldc-A
PDB Code 1ldc
Chain A

click to enlarge
Title X-RAY STRUCTURE OF TWO COMPLEXES OF THE Y143F FLAVOCYTOCHROME B2 MUTANT CRYSTALLIZED IN THE PRESENCE OF LACTATE OR PHENYL-LACTATE
Classification OXIDOREDUCTASE
Compound L-LACTATE DEHYDROGENASE
Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (CYB2_YEAST)
Sequence A:  KISPAEVAKHNKPDDCWVVINGYVYDLTRFLPNHPGGQDV
IKFNAGKDVTAIFEPLHAPNVIDKYIAPEKKLGPLQGSMP
PELVCPPYAPGETKEDIARKEQLKSLLPPLDNIINLYDFE
YLASQTLTKQAWAFYSSGANDEVTHRENHNAYHRIFFKPK
ILVDVRKVDISTDMLGSHVDVPFYVSATALCKLGNPLEGE
KDVARGCGQGVTKVPQMISTLASCSPEEIIEAAPSDKQIQ
WYQLYVNSDRKITDDLVKNVEKLGVKALFVTVDAPSLGQR
EKDMKLKALSKFIDPSLTWKDIEELKKKTKLPIVIKGVQR
TEDVIKAAEIGVSGVVLSNHGGRQLDFSRAPIEVLAETMP
ILEQRNLKDKLEVFVDGGVRRGTDVLKALCLGAKGVGLGR
PFLYANSCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAEL
KPDLLDLSTLKARTVGVPNDVLYNEVYEGPTLTEFEDA
Description


Functional site

1) chain A
residue 144
type
sequence Y
description BINDING SITE FOR RESIDUE FMN A 570
source : AC1

2) chain A
residue 195
type
sequence S
description BINDING SITE FOR RESIDUE FMN A 570
source : AC1

3) chain A
residue 196
type
sequence A
description BINDING SITE FOR RESIDUE FMN A 570
source : AC1

4) chain A
residue 197
type
sequence T
description BINDING SITE FOR RESIDUE FMN A 570
source : AC1

5) chain A
residue 198
type
sequence A
description BINDING SITE FOR RESIDUE FMN A 570
source : AC1

6) chain A
residue 228
type
sequence S
description BINDING SITE FOR RESIDUE FMN A 570
source : AC1

7) chain A
residue 252
type
sequence Q
description BINDING SITE FOR RESIDUE FMN A 570
source : AC1

8) chain A
residue 280
type
sequence T
description BINDING SITE FOR RESIDUE FMN A 570
source : AC1

9) chain A
residue 349
type
sequence K
description BINDING SITE FOR RESIDUE FMN A 570
source : AC1

10) chain A
residue 371
type
sequence S
description BINDING SITE FOR RESIDUE FMN A 570
source : AC1

11) chain A
residue 373
type
sequence H
description BINDING SITE FOR RESIDUE FMN A 570
source : AC1

12) chain A
residue 374
type
sequence G
description BINDING SITE FOR RESIDUE FMN A 570
source : AC1

13) chain A
residue 376
type
sequence R
description BINDING SITE FOR RESIDUE FMN A 570
source : AC1

14) chain A
residue 409
type
sequence D
description BINDING SITE FOR RESIDUE FMN A 570
source : AC1

15) chain A
residue 410
type
sequence G
description BINDING SITE FOR RESIDUE FMN A 570
source : AC1

16) chain A
residue 411
type
sequence G
description BINDING SITE FOR RESIDUE FMN A 570
source : AC1

17) chain A
residue 413
type
sequence R
description BINDING SITE FOR RESIDUE FMN A 570
source : AC1

18) chain A
residue 432
type
sequence G
description BINDING SITE FOR RESIDUE FMN A 570
source : AC1

19) chain A
residue 433
type
sequence R
description BINDING SITE FOR RESIDUE FMN A 570
source : AC1

20) chain A
residue 36
type
sequence L
description BINDING SITE FOR RESIDUE HEM A 560
source : AC2

21) chain A
residue 39
type
sequence F
description BINDING SITE FOR RESIDUE HEM A 560
source : AC2

22) chain A
residue 43
type
sequence H
description BINDING SITE FOR RESIDUE HEM A 560
source : AC2

23) chain A
residue 44
type
sequence P
description BINDING SITE FOR RESIDUE HEM A 560
source : AC2

24) chain A
residue 49
type
sequence V
description BINDING SITE FOR RESIDUE HEM A 560
source : AC2

25) chain A
residue 62
type
sequence F
description BINDING SITE FOR RESIDUE HEM A 560
source : AC2

26) chain A
residue 66
type
sequence H
description BINDING SITE FOR RESIDUE HEM A 560
source : AC2

27) chain A
residue 70
type
sequence V
description BINDING SITE FOR RESIDUE HEM A 560
source : AC2

28) chain A
residue 71
type
sequence I
description BINDING SITE FOR RESIDUE HEM A 560
source : AC2

29) chain A
residue 75
type
sequence I
description BINDING SITE FOR RESIDUE HEM A 560
source : AC2

30) chain A
residue 97
type
sequence Y
description BINDING SITE FOR RESIDUE HEM A 560
source : AC2

31) chain A
residue 139
type
sequence Q
description BINDING SITE FOR RESIDUE HEM A 560
source : AC2

32) chain A
residue 199
type
sequence L
description BINDING SITE FOR RESIDUE HEM A 560
source : AC2

33) chain A
residue 230
type
sequence L
description BINDING SITE FOR RESIDUE HEM A 560
source : AC2

34) chain A
residue 296
type
sequence K
description BINDING SITE FOR RESIDUE HEM A 560
source : AC2

35) chain A
residue 143
type
sequence F
description BINDING SITE FOR RESIDUE PYR A 580
source : AC3

36) chain A
residue 254
type
sequence Y
description BINDING SITE FOR RESIDUE PYR A 580
source : AC3

37) chain A
residue 289
type
sequence R
description BINDING SITE FOR RESIDUE PYR A 580
source : AC3

38) chain A
residue 373
type
sequence H
description BINDING SITE FOR RESIDUE PYR A 580
source : AC3

39) chain A
residue 376
type
sequence R
description BINDING SITE FOR RESIDUE PYR A 580
source : AC3

40) chain A
residue 254
type catalytic
sequence Y
description 102
source MCSA : MCSA1

41) chain A
residue 282
type catalytic
sequence D
description 102
source MCSA : MCSA1

42) chain A
residue 373
type catalytic
sequence H
description 102
source MCSA : MCSA1

43) chain A
residue 97
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:11914072, ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, ECO:0007744|PDB:1KBI
source Swiss-Prot : SWS_FT_FI3

44) chain A
residue 376
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:11914072, ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, ECO:0007744|PDB:1KBI
source Swiss-Prot : SWS_FT_FI3

45) chain A
residue 409
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:11914072, ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, ECO:0007744|PDB:1KBI
source Swiss-Prot : SWS_FT_FI3

46) chain A
residue 432
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:11914072, ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, ECO:0007744|PDB:1KBI
source Swiss-Prot : SWS_FT_FI3

47) chain A
residue 143
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:11914072, ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, ECO:0007744|PDB:1KBI
source Swiss-Prot : SWS_FT_FI3

48) chain A
residue 195
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:11914072, ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, ECO:0007744|PDB:1KBI
source Swiss-Prot : SWS_FT_FI3

49) chain A
residue 228
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:11914072, ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, ECO:0007744|PDB:1KBI
source Swiss-Prot : SWS_FT_FI3

50) chain A
residue 252
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:11914072, ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, ECO:0007744|PDB:1KBI
source Swiss-Prot : SWS_FT_FI3

51) chain A
residue 254
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:11914072, ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, ECO:0007744|PDB:1KBI
source Swiss-Prot : SWS_FT_FI3

52) chain A
residue 280
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:11914072, ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, ECO:0007744|PDB:1KBI
source Swiss-Prot : SWS_FT_FI3

53) chain A
residue 349
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:11914072, ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, ECO:0007744|PDB:1KBI
source Swiss-Prot : SWS_FT_FI3

54) chain A
residue 373
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:11914072, ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, ECO:0007744|PDB:1KBI
source Swiss-Prot : SWS_FT_FI3

55) chain A
residue 139
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:11914072, ECO:0007744|PDB:1KBI
source Swiss-Prot : SWS_FT_FI4

56) chain A
residue 296
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:11914072, ECO:0007744|PDB:1KBI
source Swiss-Prot : SWS_FT_FI4

57) chain A
residue 373
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000305|PubMed:17563122
source Swiss-Prot : SWS_FT_FI1

58) chain A
residue 43
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:11914072, ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, ECO:0007744|PDB:1KBI
source Swiss-Prot : SWS_FT_FI2

59) chain A
residue 66
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:11914072, ECO:0000269|PubMed:2329585, ECO:0007744|PDB:1FCB, ECO:0007744|PDB:1KBI
source Swiss-Prot : SWS_FT_FI2

60) chain A
residue 39-46
type prosite
sequence FLPNHPGG
description CYTOCHROME_B5_1 Cytochrome b5 family, heme-binding domain signature. FLPNHPGG
source prosite : PS00191

61) chain A
residue 371-377
type prosite
sequence SNHGGRQ
description FMN_HYDROXY_ACID_DH_1 FMN-dependent alpha-hydroxy acid dehydrogenases active site. SNHGGRQ
source prosite : PS00557


Display surface

Download
Links