eF-site ID 1a88-ABC
PDB Code 1a88
Chain A, B, C

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Title CHLOROPEROXIDASE L
Classification HALOPEROXIDASE
Compound CHLOROPEROXIDASE L
Source Streptomyces lividans (PRXC_STRLI)
Sequence A:  GTVTTSDGTNIFYKDWGPRDGLPVVFHHGWPLSADDWDNQ
MLFFLSHGYRVIAHDRRGHGRSDQPSTGHDMDTYAADVAA
LTEALDLRGAVHIGHSTGGGEVARYVARAEPGRVAKAVLV
SAVPPVMVKSDTNPDGLPLEVFDEFRAALAANRAQFYIDV
PSGPFYGFNREGATVSQGLIDHWWLQGMMGAANAHYECIA
AFSETDFTDDLKRIDVPVLVAHGTDDQVVPYADAAPKSAE
LLANATLKSYEGLPHGMLSTHPEVLNPDLLAFVKS
B:  GTVTTSDGTNIFYKDWGPRDGLPVVFHHGWPLSADDWDNQ
MLFFLSHGYRVIAHDRRGHGRSDQPSTGHDMDTYAADVAA
LTEALDLRGAVHIGHSTGGGEVARYVARAEPGRVAKAVLV
SAVPPVMVKSDTNPDGLPLEVFDEFRAALAANRAQFYIDV
PSGPFYGFNREGATVSQGLIDHWWLQGMMGAANAHYECIA
AFSETDFTDDLKRIDVPVLVAHGTDDQVVPYADAAPKSAE
LLANATLKSYEGLPHGMLSTHPEVLNPDLLAFVKS
C:  GTVTTSDGTNIFYKDWGPRDGLPVVFHHGWPLSADDWDNQ
MLFFLSHGYRVIAHDRRGHGRSDQPSTGHDMDTYAADVAA
LTEALDLRGAVHIGHSTGGGEVARYVARAEPGRVAKAVLV
SAVPPVMVKSDTNPDGLPLEVFDEFRAALAANRAQFYIDV
PSGPFYGFNREGATVSQGLIDHWWLQGMMGAANAHYECIA
AFSETDFTDDLKRIDVPVLVAHGTDDQVVPYADAAPKSAE
LLANATLKSYEGLPHGMLSTHPEVLNPDLLAFVKS
Description


Functional site

1) chain A
residue 96
type
sequence S
description CATALYTIC TRIAD, CHAIN A.
source : CTA

2) chain A
residue 226
type
sequence D
description CATALYTIC TRIAD, CHAIN A.
source : CTA

3) chain A
residue 255
type
sequence H
description CATALYTIC TRIAD, CHAIN A.
source : CTA

4) chain B
residue 96
type
sequence S
description CATALYTIC TRIAD, CHAIN B.
source : CTB

5) chain B
residue 226
type
sequence D
description CATALYTIC TRIAD, CHAIN B.
source : CTB

6) chain B
residue 255
type
sequence H
description CATALYTIC TRIAD, CHAIN B.
source : CTB

7) chain C
residue 96
type
sequence S
description CATALYTIC TRIAD, CHAIN C.
source : CTC

8) chain C
residue 226
type
sequence D
description CATALYTIC TRIAD, CHAIN C.
source : CTC

9) chain C
residue 255
type
sequence H
description CATALYTIC TRIAD, CHAIN C.
source : CTC

10) chain A
residue 97
type ACT_SITE
sequence T
description ACT_SITE => ECO:0000250|UniProtKB:P22862
source Swiss-Prot : SWS_FT_FI1

11) chain A
residue 227
type ACT_SITE
sequence Q
description ACT_SITE => ECO:0000250|UniProtKB:P22862
source Swiss-Prot : SWS_FT_FI1

12) chain A
residue 256
type ACT_SITE
sequence G
description ACT_SITE => ECO:0000250|UniProtKB:P22862
source Swiss-Prot : SWS_FT_FI1

13) chain B
residue 97
type ACT_SITE
sequence T
description ACT_SITE => ECO:0000250|UniProtKB:P22862
source Swiss-Prot : SWS_FT_FI1

14) chain B
residue 227
type ACT_SITE
sequence Q
description ACT_SITE => ECO:0000250|UniProtKB:P22862
source Swiss-Prot : SWS_FT_FI1

15) chain B
residue 256
type ACT_SITE
sequence G
description ACT_SITE => ECO:0000250|UniProtKB:P22862
source Swiss-Prot : SWS_FT_FI1

16) chain C
residue 97
type ACT_SITE
sequence T
description ACT_SITE => ECO:0000250|UniProtKB:P22862
source Swiss-Prot : SWS_FT_FI1

17) chain C
residue 227
type ACT_SITE
sequence Q
description ACT_SITE => ECO:0000250|UniProtKB:P22862
source Swiss-Prot : SWS_FT_FI1

18) chain C
residue 256
type ACT_SITE
sequence G
description ACT_SITE => ECO:0000250|UniProtKB:P22862
source Swiss-Prot : SWS_FT_FI1


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