eF-site ID 1r35-A
PDB Code 1r35
Chain A

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Title MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DIMER, TETRAHYDROBIOPTERIN AND 4R-FLUORO-N6-ETHANIMIDOYL-L-LYSINE
Classification OXIDOREDUCTASE
Compound Nitric oxide synthase, inducible
Source Mus musculus (Mouse) (NOS2_MOUSE)
Sequence A:  QYVRIKNWGSGEILHDTLHHKATSSCLGSIMNPKSLTRGP
RDKPTPLEELLPHAIEFINQYYGSFKEAKIEEHLARLEAV
TKEIETTGTYQLTLDELIFATKMAWRNAPRCIGRIQWSNL
QVFDARNCSTAQEMFQHICRHILYATNNGNIRSAITVFPQ
RSDGKHDFRLWNSQLIRYAGYQMPDGTIRGDAATLEFTQL
CIDLGWKPRYGRFDVLPLVLQADGQDPEVFEIPPDLVLEV
TMEHPKYEWFQELGLKWYALPAVANMLLEVGGLEFPACPF
NGWYMGTEIGVRDFCDTQRYNILEEVGRRMGLETHTLASL
WKDRAVTEINVAVLHSFQKQNVTIMDHHTASESFMKHMQN
EYRARGGCPADWIWLVPPVSGSITPVFHQEMLNYVLSPFY
YYQIEPWKTHIWQ
Description


Functional site

1) chain A
residue 97
type
sequence K
description BINDING SITE FOR RESIDUE SO4 A 903
source : AC1

2) chain A
residue 448
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 903
source : AC1

3) chain A
residue 188
type
sequence W
description BINDING SITE FOR RESIDUE HEM A 901
source : AC2

4) chain A
residue 193
type
sequence R
description BINDING SITE FOR RESIDUE HEM A 901
source : AC2

5) chain A
residue 194
type
sequence C
description BINDING SITE FOR RESIDUE HEM A 901
source : AC2

6) chain A
residue 195
type
sequence I
description BINDING SITE FOR RESIDUE HEM A 901
source : AC2

7) chain A
residue 236
type
sequence S
description BINDING SITE FOR RESIDUE HEM A 901
source : AC2

8) chain A
residue 349
type
sequence M
description BINDING SITE FOR RESIDUE HEM A 901
source : AC2

9) chain A
residue 363
type
sequence F
description BINDING SITE FOR RESIDUE HEM A 901
source : AC2

10) chain A
residue 364
type
sequence N
description BINDING SITE FOR RESIDUE HEM A 901
source : AC2

11) chain A
residue 365
type
sequence G
description BINDING SITE FOR RESIDUE HEM A 901
source : AC2

12) chain A
residue 366
type
sequence W
description BINDING SITE FOR RESIDUE HEM A 901
source : AC2

13) chain A
residue 371
type
sequence E
description BINDING SITE FOR RESIDUE HEM A 901
source : AC2

14) chain A
residue 457
type
sequence W
description BINDING SITE FOR RESIDUE HEM A 901
source : AC2

15) chain A
residue 485
type
sequence Y
description BINDING SITE FOR RESIDUE HEM A 901
source : AC2

16) chain A
residue 112
type
sequence S
description BINDING SITE FOR RESIDUE H4B A 902
source : AC3

17) chain A
residue 114
type
sequence M
description BINDING SITE FOR RESIDUE H4B A 902
source : AC3

18) chain A
residue 375
type
sequence R
description BINDING SITE FOR RESIDUE H4B A 902
source : AC3

19) chain A
residue 455
type
sequence W
description BINDING SITE FOR RESIDUE H4B A 902
source : AC3

20) chain A
residue 456
type
sequence I
description BINDING SITE FOR RESIDUE H4B A 902
source : AC3

21) chain A
residue 457
type
sequence W
description BINDING SITE FOR RESIDUE H4B A 902
source : AC3

22) chain A
residue 470
type
sequence F
description BINDING SITE FOR RESIDUE H4B A 902
source : AC3

23) chain A
residue 257
type
sequence Q
description BINDING SITE FOR RESIDUE I58 A 800
source : AC4

24) chain A
residue 341
type
sequence Y
description BINDING SITE FOR RESIDUE I58 A 800
source : AC4

25) chain A
residue 344
type
sequence P
description BINDING SITE FOR RESIDUE I58 A 800
source : AC4

26) chain A
residue 346
type
sequence V
description BINDING SITE FOR RESIDUE I58 A 800
source : AC4

27) chain A
residue 366
type
sequence W
description BINDING SITE FOR RESIDUE I58 A 800
source : AC4

28) chain A
residue 367
type
sequence Y
description BINDING SITE FOR RESIDUE I58 A 800
source : AC4

29) chain A
residue 371
type
sequence E
description BINDING SITE FOR RESIDUE I58 A 800
source : AC4

30) chain A
residue 376
type
sequence D
description BINDING SITE FOR RESIDUE I58 A 800
source : AC4

31) chain A
residue 257
type BINDING
sequence Q
description BINDING => ECO:0000250|UniProtKB:P29474
source Swiss-Prot : SWS_FT_FI4

32) chain A
residue 366
type BINDING
sequence W
description BINDING => ECO:0000250|UniProtKB:P29474
source Swiss-Prot : SWS_FT_FI4

33) chain A
residue 367
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:P29474
source Swiss-Prot : SWS_FT_FI4

34) chain A
residue 371
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P29474
source Swiss-Prot : SWS_FT_FI4

35) chain A
residue 193-200
type prosite
sequence RCIGRIQW
description NOS Nitric oxide synthase (NOS) signature. RCIGRIqW
source prosite : PS60001

36) chain A
residue 375
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:10562539, ECO:0000269|PubMed:10769116, ECO:0000269|PubMed:11669619, ECO:0000269|PubMed:12437348, ECO:0000269|PubMed:12464241, ECO:0000269|PubMed:9516116, ECO:0007744|PDB:1DF1, ECO:0007744|PDB:1DWX, ECO:0007744|PDB:1JWJ, ECO:0007744|PDB:1JWK, ECO:0007744|PDB:1M8D, ECO:0007744|PDB:1M8E, ECO:0007744|PDB:1M8H, ECO:0007744|PDB:1M8I, ECO:0007744|PDB:1M9T, ECO:0007744|PDB:1N2N, ECO:0007744|PDB:1NOD, ECO:0007744|PDB:1QOM, ECO:0007744|PDB:3NOD
source Swiss-Prot : SWS_FT_FI5

37) chain A
residue 456
type BINDING
sequence I
description BINDING => ECO:0000269|PubMed:10562539, ECO:0000269|PubMed:12437348, ECO:0000269|PubMed:12464241, ECO:0007744|PDB:1DF1, ECO:0007744|PDB:1M9T, ECO:0007744|PDB:1N2N
source Swiss-Prot : SWS_FT_FI6

38) chain A
residue 457
type BINDING
sequence W
description BINDING => ECO:0000269|PubMed:10562539, ECO:0000269|PubMed:10769116, ECO:0000269|PubMed:12437348, ECO:0000269|PubMed:12464241, ECO:0000269|PubMed:9516116, ECO:0007744|PDB:1DF1, ECO:0007744|PDB:1DWX, ECO:0007744|PDB:1M8D, ECO:0007744|PDB:1M8E, ECO:0007744|PDB:1M8I, ECO:0007744|PDB:1M9T, ECO:0007744|PDB:1N2N, ECO:0007744|PDB:1NOD, ECO:0007744|PDB:1QOM, ECO:0007744|PDB:2NOD, ECO:0007744|PDB:3NOD
source Swiss-Prot : SWS_FT_FI7

39) chain A
residue 470
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:10562539, ECO:0000269|PubMed:10769116, ECO:0000269|PubMed:11669619, ECO:0000269|PubMed:12437348, ECO:0000269|PubMed:12464241, ECO:0000269|PubMed:9516116, ECO:0007744|PDB:1DF1, ECO:0007744|PDB:1DWX, ECO:0007744|PDB:1JWJ, ECO:0007744|PDB:1JWK, ECO:0007744|PDB:1M8D, ECO:0007744|PDB:1M8E, ECO:0007744|PDB:1M8H, ECO:0007744|PDB:1M8I, ECO:0007744|PDB:1N2N, ECO:0007744|PDB:1NOD, ECO:0007744|PDB:1QOM, ECO:0007744|PDB:2NOD, ECO:0007744|PDB:3NOD
source Swiss-Prot : SWS_FT_FI8

40) chain A
residue 485
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:10562539, ECO:0000269|PubMed:10769116, ECO:0000269|PubMed:9516116, ECO:0007744|PDB:1DF1, ECO:0007744|PDB:1DWX, ECO:0007744|PDB:1NOD, ECO:0007744|PDB:1QOM, ECO:0007744|PDB:2NOD, ECO:0007744|PDB:3NOD
source Swiss-Prot : SWS_FT_FI9

41) chain A
residue 112
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:10562539, ECO:0000269|PubMed:10769116, ECO:0000269|PubMed:11669619, ECO:0000269|PubMed:12437348, ECO:0000269|PubMed:12464241, ECO:0000269|PubMed:9516116, ECO:0007744|PDB:1DF1, ECO:0007744|PDB:1DWX, ECO:0007744|PDB:1JWJ, ECO:0007744|PDB:1M8D, ECO:0007744|PDB:1M8E, ECO:0007744|PDB:1M8H, ECO:0007744|PDB:1M8I, ECO:0007744|PDB:1M9T, ECO:0007744|PDB:1N2N, ECO:0007744|PDB:1NOD, ECO:0007744|PDB:1QOM, ECO:0007744|PDB:2NOD, ECO:0007744|PDB:3NOD
source Swiss-Prot : SWS_FT_FI2

42) chain A
residue 109
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:10562539, ECO:0000269|PubMed:10769116, ECO:0000269|PubMed:12464241, ECO:0007744|PDB:1DF1, ECO:0007744|PDB:1DWV, ECO:0007744|PDB:1DWW, ECO:0007744|PDB:1N2N
source Swiss-Prot : SWS_FT_FI1

43) chain A
residue 194
type BINDING
sequence C
description axial binding residue => ECO:0000269|PubMed:10562539, ECO:0000269|PubMed:10769116, ECO:0000269|PubMed:11669619, ECO:0000269|PubMed:12437348, ECO:0000269|PubMed:12464241, ECO:0000269|PubMed:9334294, ECO:0000269|PubMed:9516116, ECO:0007744|PDB:1DF1, ECO:0007744|PDB:1DWV, ECO:0007744|PDB:1DWW, ECO:0007744|PDB:1DWX, ECO:0007744|PDB:1JWJ, ECO:0007744|PDB:1JWK, ECO:0007744|PDB:1M8D, ECO:0007744|PDB:1M8E, ECO:0007744|PDB:1M8H, ECO:0007744|PDB:1M8I, ECO:0007744|PDB:1M9T, ECO:0007744|PDB:1N2N, ECO:0007744|PDB:1NOC, ECO:0007744|PDB:1NOD, ECO:0007744|PDB:1NOS, ECO:0007744|PDB:1QOM, ECO:0007744|PDB:2NOD, ECO:0007744|PDB:2NOS, ECO:0007744|PDB:3NOD
source Swiss-Prot : SWS_FT_FI3


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