eF-site ID 3erh-A
PDB Code 3erh
Chain A

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Title First structural evidence of substrate specificity in mammalian peroxidases: Crystal structures of substrate complexes with lactoperoxidases from two different species
Classification OXIDOREDUCTASE
Compound Lactoperoxidase
Source ORGANISM_COMMON: Domestic water buffalo; ORGANISM_SCIENTIFIC: Bubalus bubalis;
Sequence A:  SWEVGCGAPVPLVKCDENSPYRTITGDCNNRRSPALGAAN
RALARWLPAEYEDGLALPFGWTQRKTRNGFRVPLAREVSN
KIVGYLDEEGVLDQNRSLLFMQWGQIVDHDLDFAPETELG
SNEHSKTQCEEYCIQGDNCFPIMFPKNDPKLKTQGKCMPF
FRAGFVCPTPPYQSLAREQINAVTSFLDASLVYGSEPXLA
SRLRNLSSPLGLMAVNQEAWDHGLAYLPFNNKKPSPCEFI
NTTARVPCFLAGDFRASEQILLATAHTLLLREHNRLAREL
KKLNPHWNGEKLYQEARKILGAFIQIITFRDYLPIVLGSE
MQKWIPPYQGYNNSVDPRISNVFTFAFRFGHMEVPSTVSR
LDENYQPWGPEAELPLHTLFFNTWRIIKDGGIDPLTRGLL
AKKSKLMNQDKMVTSELRNKLFQPTHKIHGFDLAAINLQR
CRDHGMPGYNSWRGFCGLSQPKTLKGLQTVLKNKILAKKL
MDLYKTPDNIDIWIGGNAEPMVERGRVGPLLACLLGRQFQ
QIRDGDRFWWENPGVFTEKQRDSLQKFSFSRLICDNTHIT
KVPLHAFQANNYPHDFVDCSTVDKLDLSPWASREN
Description


Functional site
1) chain A
residue 109
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000250|UniProtKB:P05164, ECO:0000255|PROSITE-ProRule:PRU00298
source Swiss-Prot : SWS_FT_FI1
2) chain A
residue 108
type BINDING
sequence D
description covalent => ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5, ECO:0000269|Ref.6
source Swiss-Prot : SWS_FT_FI2
3) chain A
residue 258
type BINDING
sequence E
description covalent => ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5, ECO:0000269|Ref.6
source Swiss-Prot : SWS_FT_FI2
4) chain A
residue 184
type BINDING
sequence T
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5, ECO:0000269|Ref.6
source Swiss-Prot : SWS_FT_FI3
5) chain A
residue 186
type BINDING
sequence F
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5, ECO:0000269|Ref.6
source Swiss-Prot : SWS_FT_FI3
6) chain A
residue 188
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5, ECO:0000269|Ref.6
source Swiss-Prot : SWS_FT_FI3
7) chain A
residue 190
type BINDING
sequence S
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5, ECO:0000269|Ref.6
source Swiss-Prot : SWS_FT_FI3
8) chain A
residue 110
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5, ECO:0000269|Ref.6
source Swiss-Prot : SWS_FT_FI3
9) chain A
residue 198
type MOD_RES
sequence X
description Phosphoserine => ECO:0000269|PubMed:19339248, ECO:0000269|Ref.6
source Swiss-Prot : SWS_FT_FI6
10) chain A
residue 365
type MOD_RES
sequence Y
description 3'-nitrotyrosine => ECO:0000250|UniProtKB:P11678
source Swiss-Prot : SWS_FT_FI7
11) chain A
residue 95
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (high mannose) asparagine; alternate => ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:30296068, ECO:0000269|Ref.5, ECO:0000269|Ref.6
source Swiss-Prot : SWS_FT_FI8
12) chain A
residue 205
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:30296068, ECO:0000269|Ref.5, ECO:0000269|Ref.6
source Swiss-Prot : SWS_FT_FI9
13) chain A
residue 241
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19339248, ECO:0000269|Ref.5, ECO:0000269|Ref.6
source Swiss-Prot : SWS_FT_FI10
14) chain A
residue 332
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (hybrid) asparagine; alternate => ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:30296068, ECO:0000269|Ref.5, ECO:0000269|Ref.6
source Swiss-Prot : SWS_FT_FI11
15) chain A
residue 105
type catalytic
sequence Q
description 944
source MCSA : MCSA1
16) chain A
residue 108
type catalytic
sequence D
description 944
source MCSA : MCSA1
17) chain A
residue 110
type catalytic
sequence D
description 944
source MCSA : MCSA1
18) chain A
residue 184
type catalytic
sequence T
description 944
source MCSA : MCSA1
19) chain A
residue 186
type catalytic
sequence F
description 944
source MCSA : MCSA1
20) chain A
residue 188
type catalytic
sequence D
description 944
source MCSA : MCSA1
21) chain A
residue 190
type catalytic
sequence S
description 944
source MCSA : MCSA1
22) chain A
residue 258
type catalytic
sequence E
description 944
source MCSA : MCSA1
23) chain A
residue 351
type catalytic
sequence H
description 944
source MCSA : MCSA1
24) chain A
residue 255
type SITE
sequence R
description Transition state stabilizer => ECO:0000250|UniProtKB:P05164, ECO:0000255|PROSITE-ProRule:PRU00298
source Swiss-Prot : SWS_FT_FI5
25) chain A
residue 351
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:19339248
source Swiss-Prot : SWS_FT_FI4

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