eF-site ID 1lsj-B
PDB Code 1lsj
Chain B

click to enlarge
Title Crystal Structure of the E110Q Mutant of L-3-Hydroxyacyl-CoA Dehydrogenase in Complex with NAD
Classification OXIDOREDUCTASE
Compound 3-HYDROXYACYL-COA DEHYDROGENASE
Source Homo sapiens (Human) (HCDH_HUMAN)
Sequence B:  KIIVKHVTVIGGGLMGAGIAQVAAATGHTVVLVDQTEDIL
AKSKKGIEESLRKVAKKKFAENPKAGDEFVEKTLSTIATS
TDAASVVHSTDLVVEAIVQNLKVKNELFKRLDKFAAEHTI
FASNTSSLQITSIANATTRQDRFAGLHFFNPVPVMKLVEV
IKTPMTSQKTFESLVDFSKALGKHPVSCKDTPGFIVNRLL
VPYLMEAIRLYERGDASKEDIDTAMKLGAGYPMGPFELLD
YVGLDTTKFIVDGWHEMDAENPLHQPSPSLNKLVAENKFG
KKTGEGFYKYK
Description


Functional site

1) chain B
residue 24
type
sequence G
description BINDING SITE FOR RESIDUE NAD B 750
source : AC2

2) chain B
residue 25
type
sequence L
description BINDING SITE FOR RESIDUE NAD B 750
source : AC2

3) chain B
residue 26
type
sequence M
description BINDING SITE FOR RESIDUE NAD B 750
source : AC2

4) chain B
residue 45
type
sequence D
description BINDING SITE FOR RESIDUE NAD B 750
source : AC2

5) chain B
residue 46
type
sequence Q
description BINDING SITE FOR RESIDUE NAD B 750
source : AC2

6) chain B
residue 107
type
sequence A
description BINDING SITE FOR RESIDUE NAD B 750
source : AC2

7) chain B
residue 108
type
sequence I
description BINDING SITE FOR RESIDUE NAD B 750
source : AC2

8) chain B
residue 109
type
sequence V
description BINDING SITE FOR RESIDUE NAD B 750
source : AC2

9) chain B
residue 110
type
sequence Q
description BINDING SITE FOR RESIDUE NAD B 750
source : AC2

10) chain B
residue 115
type
sequence K
description BINDING SITE FOR RESIDUE NAD B 750
source : AC2

11) chain B
residue 135
type
sequence N
description BINDING SITE FOR RESIDUE NAD B 750
source : AC2

12) chain B
residue 137
type
sequence S
description BINDING SITE FOR RESIDUE NAD B 750
source : AC2

13) chain B
residue 143
type catalytic
sequence S
description 336
source MCSA : MCSA2

14) chain B
residue 164
type catalytic
sequence P
description 336
source MCSA : MCSA2

15) chain B
residue 176
type catalytic
sequence M
description 336
source MCSA : MCSA2

16) chain B
residue 214
type catalytic
sequence Y
description 336
source MCSA : MCSA2

17) chain B
residue 116
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044
source Swiss-Prot : SWS_FT_FI1

18) chain B
residue 121
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044
source Swiss-Prot : SWS_FT_FI1

19) chain B
residue 143
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044
source Swiss-Prot : SWS_FT_FI1

20) chain B
residue 167
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044
source Swiss-Prot : SWS_FT_FI1

21) chain B
residue 299
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044
source Swiss-Prot : SWS_FT_FI1

22) chain B
residue 28
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044
source Swiss-Prot : SWS_FT_FI1

23) chain B
residue 51
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:10231530, ECO:0000269|PubMed:10840044
source Swiss-Prot : SWS_FT_FI1

24) chain B
residue 67
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:10840044
source Swiss-Prot : SWS_FT_FI2

25) chain B
residue 74
type BINDING
sequence P
description BINDING => ECO:0000269|PubMed:10840044
source Swiss-Prot : SWS_FT_FI2

26) chain B
residue 164
type SITE
sequence P
description Important for catalytic activity => ECO:0000305
source Swiss-Prot : SWS_FT_FI3

27) chain B
residue 74
type MOD_RES
sequence P
description N6-succinyllysine => ECO:0000250|UniProtKB:Q61425
source Swiss-Prot : SWS_FT_FI4

28) chain B
residue 200
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q61425
source Swiss-Prot : SWS_FT_FI4

29) chain B
residue 81
type MOD_RES
sequence V
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425
source Swiss-Prot : SWS_FT_FI5

30) chain B
residue 130
type MOD_RES
sequence T
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425
source Swiss-Prot : SWS_FT_FI5

31) chain B
residue 179
type MOD_RES
sequence Q
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425
source Swiss-Prot : SWS_FT_FI5

32) chain B
residue 186
type MOD_RES
sequence V
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425
source Swiss-Prot : SWS_FT_FI5

33) chain B
residue 196
type MOD_RES
sequence P
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425
source Swiss-Prot : SWS_FT_FI5

34) chain B
residue 206
type MOD_RES
sequence I
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425
source Swiss-Prot : SWS_FT_FI5

35) chain B
residue 235
type MOD_RES
sequence A
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425
source Swiss-Prot : SWS_FT_FI5

36) chain B
residue 75
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q61425
source Swiss-Prot : SWS_FT_FI5

37) chain B
residue 119
type MOD_RES
sequence F
description N6-acetyllysine => ECO:0000250|UniProtKB:Q61425
source Swiss-Prot : SWS_FT_FI6

38) chain B
residue 173
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:Q61425
source Swiss-Prot : SWS_FT_FI6

39) chain B
residue 121
type MOD_RES
sequence R
description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674
source Swiss-Prot : SWS_FT_FI7


Display surface

Download
Links