eF-site ID 4au9-AB
PDB Code 4au9
Chain A, B

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Title Crystal Structure of a Fungal DyP-Type Peroxidase from Auricularia auricula-judae
Classification OXIDOREDUCTASE
Compound DYP-TYPE PEROXIDASE I
Source ORGANISM_COMMON: EAR FUNGUS; ORGANISM_SCIENTIFIC: AURICULARIA AURICULA-JUDAE;
Sequence A:  ATSLNTDDIQGDILVGMHKQKQLFYFFAINDPATFKTFLA
SDIAPVVASVTQLSNVATQPLVALNIAFSNTGLLALGVTD
NLGDSLFANGQAKDATSFKESTSSWVPQFAGTGIHGVIIL
ASDTTDLIDQQVASIESTFGSSISKLYSLSASIRPGNEAG
HEMFGFLDGIAQPAINGFNTPLPGQNIVDAGVIITGATND
PITRPSWAVGGSFLAFRQLEQLVPEFNKYLLDNAPAGSGS
LQARADLLGARMVGRWKSGAPIDLTPTADDPALGADAQRN
NNFTYSHAGFDLGSDQSHCPFSAHIRKTRPRADLGGSLTP
PNLSAGANSIMRSGIPYGPEVTSAESASNTTTQERGLAFV
AYQAQLSQGFHFLQQTWADNANFPPGKTPATVGLDPIIGQ
NNGQPRVVNGLLPSNSSASLSIPQFVVSHGGEYFFSPPIS
AIGGRLSA
B:  ATSLNTDDIQGDILVGMHKQKQLFYFFAINDPATFKTFLA
SDIAPVVASVTQLSNVATQPLVALNIAFSNTGLLALGVTD
NLGDSLFANGQAKDATSFKESTSSWVPQFAGTGIHGVIIL
ASDTTDLIDQQVASIESTFGSSISKLYSLSASIRPGNEAG
HEMFGFLDGIAQPAINGFNTPLPGQNIVDAGVIITGATND
PITRPSWAVGGSFLAFRQLEQLVPEFNKYLLDNAPAGSGS
LQARADLLGARMVGRWKSGAPIDLTPTADDPALGADAQRN
NNFTYSHAGFDLGSDQSHCPFSAHIRKTRPRADLGGSLTP
PNLSAGANSIMRSGIPYGPEVTSAESASNTTTQERGLAFV
AYQAQLSQGFHFLQQTWADNANFPPGKTPATVGLDPIIGQ
NNGQPRVVNGLLPSNSSASLSIPQFVVSHGGEYFFSPPIS
AIGGRLSA
Description


Functional site

1) chain A
residue 304
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:23235158, ECO:0000269|PubMed:25495127, ECO:0000269|PubMed:25542606, ECO:0000269|DOI:10.1039/c6cy00539j, ECO:0000269|Ref.8, ECO:0007744|PDB:4AU9, ECO:0007744|PDB:4UZI, ECO:0007744|PDB:4W7J, ECO:0007744|PDB:4W7K, ECO:0007744|PDB:4W7L, ECO:0007744|PDB:4W7M, ECO:0007744|PDB:4W7N, ECO:0007744|PDB:4W7O, ECO:0007744|PDB:5AG0, ECO:0007744|PDB:5IKD, ECO:0007744|PDB:5IKG
source Swiss-Prot : SWS_FT_FI2

2) chain B
residue 304
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:23235158, ECO:0000269|PubMed:25495127, ECO:0000269|PubMed:25542606, ECO:0000269|DOI:10.1039/c6cy00539j, ECO:0000269|Ref.8, ECO:0007744|PDB:4AU9, ECO:0007744|PDB:4UZI, ECO:0007744|PDB:4W7J, ECO:0007744|PDB:4W7K, ECO:0007744|PDB:4W7L, ECO:0007744|PDB:4W7M, ECO:0007744|PDB:4W7N, ECO:0007744|PDB:4W7O, ECO:0007744|PDB:5AG0, ECO:0007744|PDB:5IKD, ECO:0007744|PDB:5IKG
source Swiss-Prot : SWS_FT_FI2

3) chain A
residue 168
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000269|PubMed:23235158
source Swiss-Prot : SWS_FT_FI1

4) chain B
residue 168
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000269|PubMed:23235158
source Swiss-Prot : SWS_FT_FI1

5) chain A
residue 282
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23235158, ECO:0000269|PubMed:25542606, ECO:0000269|Ref.8, ECO:0007744|PDB:4AU9, ECO:0007744|PDB:4UZI, ECO:0007744|PDB:5AG0, ECO:0007744|PDB:5AG1
source Swiss-Prot : SWS_FT_FI3

6) chain A
residue 349
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23235158, ECO:0000269|PubMed:25542606, ECO:0000269|Ref.8, ECO:0007744|PDB:4AU9, ECO:0007744|PDB:4UZI, ECO:0007744|PDB:5AG0, ECO:0007744|PDB:5AG1
source Swiss-Prot : SWS_FT_FI3

7) chain A
residue 415
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23235158, ECO:0000269|PubMed:25542606, ECO:0000269|Ref.8, ECO:0007744|PDB:4AU9, ECO:0007744|PDB:4UZI, ECO:0007744|PDB:5AG0, ECO:0007744|PDB:5AG1
source Swiss-Prot : SWS_FT_FI3

8) chain B
residue 282
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23235158, ECO:0000269|PubMed:25542606, ECO:0000269|Ref.8, ECO:0007744|PDB:4AU9, ECO:0007744|PDB:4UZI, ECO:0007744|PDB:5AG0, ECO:0007744|PDB:5AG1
source Swiss-Prot : SWS_FT_FI3

9) chain B
residue 349
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23235158, ECO:0000269|PubMed:25542606, ECO:0000269|Ref.8, ECO:0007744|PDB:4AU9, ECO:0007744|PDB:4UZI, ECO:0007744|PDB:5AG0, ECO:0007744|PDB:5AG1
source Swiss-Prot : SWS_FT_FI3

10) chain B
residue 415
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23235158, ECO:0000269|PubMed:25542606, ECO:0000269|Ref.8, ECO:0007744|PDB:4AU9, ECO:0007744|PDB:4UZI, ECO:0007744|PDB:5AG0, ECO:0007744|PDB:5AG1
source Swiss-Prot : SWS_FT_FI3

11) chain A
residue 322
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
source Swiss-Prot : SWS_FT_FI4

12) chain B
residue 322
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
source Swiss-Prot : SWS_FT_FI4

13) chain A
residue 160-174
type prosite
sequence GHEMFGFLDGIAQPA
description ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEmFGFldgiAqpA
source prosite : PS00059


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