eF-site ID 1v3u-A
PDB Code 1v3u
Chain A

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Title Crystal structure of leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase in apo form
Classification OXIDOREDUCTASE
Compound leukotriene b4 12-hydroxydehydrogenase/prostaglandin 15-keto reductase
Source Cavia porcellus (Guinea pig) (Q9EQZ5_CAVPO)
Sequence A:  FMVKAKSWTLKKPTQSDFELKTVELPPLKNGEVLLEALFL
SVDPYMRIASKRLKEGAVMMGQQVARVVESKNSAFPAGSI
VLAQSGWTTHFISDGKGLEKLLWPDKLPLSLALGTIGMPG
LTAYFGLLEVCGVKGGETVLVSAAAGAVGSVVGQIAKLKG
CKVVGAAGSDEKIAYLKQIGFDAAFNYKTVNSLEEALKKA
SPDGYDCYFDNVGGEFLNTVLSQMKDFGKIAICGAISLPP
GPSPESIIYKQLRIEGFIVYRWQGDVREKALRDLMKWVLE
GKIQYHEHVTKGFENMPAAFIEMLNGANLGKAVVTA
Description


Functional site

1) chain A
residue 324
type
sequence K
description BINDING SITE FOR RESIDUE CL A 1001
source : AC1

2) chain A
residue 325
type
sequence A
description BINDING SITE FOR RESIDUE CL A 1001
source : AC1

3) chain A
residue 70
type
sequence R
description BINDING SITE FOR RESIDUE CL A 1004
source : AC4

4) chain A
residue 72
type
sequence V
description BINDING SITE FOR RESIDUE CL A 1004
source : AC4

5) chain A
residue 149
type
sequence A
description BINDING SITE FOR RESIDUE CL A 1006
source : AC6

6) chain A
residue 151
type
sequence A
description BINDING SITE FOR RESIDUE CL A 1006
source : AC6

7) chain A
residue 173
type
sequence A
description BINDING SITE FOR RESIDUE CL A 1006
source : AC6

8) chain A
residue 178
type
sequence K
description BINDING SITE FOR RESIDUE CL A 1006
source : AC6

9) chain A
residue 18
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:Q14914
source Swiss-Prot : SWS_FT_FI2

10) chain A
residue 20
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:Q14914
source Swiss-Prot : SWS_FT_FI3

11) chain A
residue 152
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:15007077
source Swiss-Prot : SWS_FT_FI1

12) chain A
residue 178
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:15007077
source Swiss-Prot : SWS_FT_FI1

13) chain A
residue 193
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:15007077
source Swiss-Prot : SWS_FT_FI1

14) chain A
residue 217
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:15007077
source Swiss-Prot : SWS_FT_FI1

15) chain A
residue 239
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:15007077
source Swiss-Prot : SWS_FT_FI1

16) chain A
residue 270
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:15007077
source Swiss-Prot : SWS_FT_FI1

17) chain A
residue 321
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:15007077
source Swiss-Prot : SWS_FT_FI1

18) chain A
residue 178
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:Q91YR9
source Swiss-Prot : SWS_FT_FI4


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