eF-site ID 5qie-A
PDB Code 5qie
Chain A

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Title PanDDA analysis group deposition of models with modelled events (e.g. bound ligands) -- Crystal Structure of HAO1 in complex with Z2856434894
Classification OXIDOREDUCTASE
Compound Hydroxyacid oxidase 1
Source (HAOX1_HUMAN)
Sequence A:  RLICINDYEQHAKSVLPKSIYDYYRSGANDEETLADNIAA
FSRWKLYPRMLRNVAETDLSTSVLGQRVSMPICVGATAMQ
RMAHVDGELATVRACQSLGTGMMLSSWATSSIEEVAEAGP
EALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVDTPY
LGNRLDDVRNRFKLPPQLRMKNFETSTLSFSPDSGLAAYV
AKAIDPSISWEDIKWLRRLTSLPIVAKGILRGDDAREAVK
HGLNGILVSNHGARQLDGVPATIDVLPEIVEAVEGKVEVF
LDGGVRKGTDVLKALALGAKAVFVGRPIVWGLAFQGEKGV
QDVLEILKEEFRLAMALSGCQNVKVIDKTLVRK
Description


Functional site

1) chain A
residue 26
type
sequence Y
description binding site for residue FMN A 401
source : AC1

2) chain A
residue 27
type
sequence Y
description binding site for residue FMN A 401
source : AC1

3) chain A
residue 79
type
sequence A
description binding site for residue FMN A 401
source : AC1

4) chain A
residue 80
type
sequence T
description binding site for residue FMN A 401
source : AC1

5) chain A
residue 81
type
sequence A
description binding site for residue FMN A 401
source : AC1

6) chain A
residue 108
type
sequence S
description binding site for residue FMN A 401
source : AC1

7) chain A
residue 130
type
sequence Q
description binding site for residue FMN A 401
source : AC1

8) chain A
residue 132
type
sequence Y
description binding site for residue FMN A 401
source : AC1

9) chain A
residue 158
type
sequence T
description binding site for residue FMN A 401
source : AC1

10) chain A
residue 236
type
sequence K
description binding site for residue FMN A 401
source : AC1

11) chain A
residue 258
type
sequence S
description binding site for residue FMN A 401
source : AC1

12) chain A
residue 260
type
sequence H
description binding site for residue FMN A 401
source : AC1

13) chain A
residue 261
type
sequence G
description binding site for residue FMN A 401
source : AC1

14) chain A
residue 263
type
sequence R
description binding site for residue FMN A 401
source : AC1

15) chain A
residue 291
type
sequence D
description binding site for residue FMN A 401
source : AC1

16) chain A
residue 292
type
sequence G
description binding site for residue FMN A 401
source : AC1

17) chain A
residue 293
type
sequence G
description binding site for residue FMN A 401
source : AC1

18) chain A
residue 295
type
sequence R
description binding site for residue FMN A 401
source : AC1

19) chain A
residue 314
type
sequence G
description binding site for residue FMN A 401
source : AC1

20) chain A
residue 315
type
sequence R
description binding site for residue FMN A 401
source : AC1

21) chain A
residue 6
type
sequence I
description binding site for residue GWV A 402
source : AC2

22) chain A
residue 166
type
sequence N
description binding site for residue GWV A 402
source : AC2

23) chain A
residue 331
type
sequence D
description binding site for residue GWV A 402
source : AC2

24) chain A
residue 258-264
type prosite
sequence SNHGARQ
description FMN_HYDROXY_ACID_DH_1 FMN-dependent alpha-hydroxy acid dehydrogenases active site. SNHGARQ
source prosite : PS00557

25) chain A
residue 230
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI10

26) chain A
residue 194
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:Q9WU19
source Swiss-Prot : SWS_FT_FI9

27) chain A
residue 260
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00683
source Swiss-Prot : SWS_FT_FI1

28) chain A
residue 260
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:18215067, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDU
source Swiss-Prot : SWS_FT_FI2

29) chain A
residue 263
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:18215067, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDU
source Swiss-Prot : SWS_FT_FI2

30) chain A
residue 132
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:18215067, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDU
source Swiss-Prot : SWS_FT_FI2

31) chain A
residue 26
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:18215067, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDU
source Swiss-Prot : SWS_FT_FI2

32) chain A
residue 130
type BINDING
sequence Q
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00683, ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120, ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2W0U
source Swiss-Prot : SWS_FT_FI5

33) chain A
residue 167
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:18215067, ECO:0000269|Ref.11, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDU
source Swiss-Prot : SWS_FT_FI6

34) chain A
residue 291
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120, ECO:0000269|Ref.11, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2RDW, ECO:0007744|PDB:2W0U
source Swiss-Prot : SWS_FT_FI7

35) chain A
residue 314
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120, ECO:0000269|Ref.11, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2RDW, ECO:0007744|PDB:2W0U
source Swiss-Prot : SWS_FT_FI7

36) chain A
residue 258
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120, ECO:0000269|Ref.11, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2RDW, ECO:0007744|PDB:2W0U
source Swiss-Prot : SWS_FT_FI7

37) chain A
residue 184
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9WU19
source Swiss-Prot : SWS_FT_FI8

38) chain A
residue 79
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120, ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2RDW, ECO:0007744|PDB:2W0U
source Swiss-Prot : SWS_FT_FI3

39) chain A
residue 236
type BINDING
sequence K
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00683, ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120, ECO:0000269|Ref.11, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2RDW, ECO:0007744|PDB:2W0U
source Swiss-Prot : SWS_FT_FI4

40) chain A
residue 108
type BINDING
sequence S
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00683, ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120, ECO:0000269|Ref.11, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2RDW, ECO:0007744|PDB:2W0U
source Swiss-Prot : SWS_FT_FI4

41) chain A
residue 158
type BINDING
sequence T
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00683, ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120, ECO:0000269|Ref.11, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2RDW, ECO:0007744|PDB:2W0U
source Swiss-Prot : SWS_FT_FI4


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