eF-site ID 1pbd-A
PDB Code 1pbd
Chain A

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Title CRYSTAL STRUCTURES OF WILD-TYPE P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE, 2,4-DIHYDROXYBENZOATE AND 2-HYDROXY-4-AMINOBENZOATE AND OF THE TRY222ALA MUTANT, COMPLEXED WITH 2-HYDROXY-4-AMINOBENZOATE. EVIDENCE FOR A PROTON CHANNEL AND A NEW BINDING MODE OF THE FLAVIN RING
Classification OXIDOREDUCTASE
Compound P-HYDROXYBENZOATE HYDROXYLASE
Source Pseudomonas fluorescens (PHHY_PSEFL)
Sequence A:  MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVL
GRIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFA
GQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREASGATT
VYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDG
FHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELI
YANHPRGFALCSQRSATRSRYYVQVPLTEKVEDWSDERFW
TELKARLPAEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGR
LFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREG
RGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFS
QRIQQTELEYYLGSEAGLATIAENYVGLPYE
Description


Functional site
1) chain A
residue 8
type
sequence I
description BINDING SITE FOR RESIDUE FAD A 395
source : AC1
2) chain A
residue 9
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 395
source : AC1
3) chain A
residue 11
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 395
source : AC1
4) chain A
residue 12
type
sequence P
description BINDING SITE FOR RESIDUE FAD A 395
source : AC1
5) chain A
residue 13
type
sequence S
description BINDING SITE FOR RESIDUE FAD A 395
source : AC1
6) chain A
residue 31
type
sequence L
description BINDING SITE FOR RESIDUE FAD A 395
source : AC1
7) chain A
residue 32
type
sequence E
description BINDING SITE FOR RESIDUE FAD A 395
source : AC1
8) chain A
residue 33
type
sequence R
description BINDING SITE FOR RESIDUE FAD A 395
source : AC1
9) chain A
residue 42
type
sequence R
description BINDING SITE FOR RESIDUE FAD A 395
source : AC1
10) chain A
residue 44
type
sequence R
description BINDING SITE FOR RESIDUE FAD A 395
source : AC1
11) chain A
residue 45
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 395
source : AC1
12) chain A
residue 46
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 395
source : AC1
13) chain A
residue 47
type
sequence V
description BINDING SITE FOR RESIDUE FAD A 395
source : AC1
14) chain A
residue 102
type
sequence Q
description BINDING SITE FOR RESIDUE FAD A 395
source : AC1
15) chain A
residue 158
type
sequence C
description BINDING SITE FOR RESIDUE FAD A 395
source : AC1
16) chain A
residue 159
type
sequence D
description BINDING SITE FOR RESIDUE FAD A 395
source : AC1
17) chain A
residue 160
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 395
source : AC1
18) chain A
residue 285
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 395
source : AC1
19) chain A
residue 286
type
sequence D
description BINDING SITE FOR RESIDUE FAD A 395
source : AC1
20) chain A
residue 296
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 395
source : AC1
21) chain A
residue 297
type
sequence K
description BINDING SITE FOR RESIDUE FAD A 395
source : AC1
22) chain A
residue 298
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 395
source : AC1
23) chain A
residue 299
type
sequence L
description BINDING SITE FOR RESIDUE FAD A 395
source : AC1
24) chain A
residue 300
type
sequence N
description BINDING SITE FOR RESIDUE FAD A 395
source : AC1
25) chain A
residue 44
type
sequence R
description BINDING SITE FOR RESIDUE PAB A 396
source : AC2
26) chain A
residue 47
type
sequence V
description BINDING SITE FOR RESIDUE PAB A 396
source : AC2
27) chain A
residue 185
type
sequence W
description BINDING SITE FOR RESIDUE PAB A 396
source : AC2
28) chain A
residue 201
type
sequence Y
description BINDING SITE FOR RESIDUE PAB A 396
source : AC2
29) chain A
residue 212
type
sequence S
description BINDING SITE FOR RESIDUE PAB A 396
source : AC2
30) chain A
residue 214
type
sequence R
description BINDING SITE FOR RESIDUE PAB A 396
source : AC2
31) chain A
residue 222
type
sequence Y
description BINDING SITE FOR RESIDUE PAB A 396
source : AC2
32) chain A
residue 293
type
sequence P
description BINDING SITE FOR RESIDUE PAB A 396
source : AC2
33) chain A
residue 294
type
sequence T
description BINDING SITE FOR RESIDUE PAB A 396
source : AC2
34) chain A
residue 13
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:10025942, ECO:0000269|PubMed:10493859, ECO:0000269|PubMed:2553983, ECO:0000269|PubMed:2819062, ECO:0000269|PubMed:3351945, ECO:0000269|PubMed:7520279, ECO:0000269|PubMed:7628466, ECO:0000269|PubMed:7756982, ECO:0000269|PubMed:9578477, ECO:0000269|PubMed:9694855
source Swiss-Prot : SWS_FT_FI1
35) chain A
residue 299
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:10025942, ECO:0000269|PubMed:10493859, ECO:0000269|PubMed:2553983, ECO:0000269|PubMed:2819062, ECO:0000269|PubMed:3351945, ECO:0000269|PubMed:7520279, ECO:0000269|PubMed:7628466, ECO:0000269|PubMed:7756982, ECO:0000269|PubMed:9578477, ECO:0000269|PubMed:9694855
source Swiss-Prot : SWS_FT_FI1
36) chain A
residue 32
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10025942, ECO:0000269|PubMed:10493859, ECO:0000269|PubMed:2553983, ECO:0000269|PubMed:2819062, ECO:0000269|PubMed:3351945, ECO:0000269|PubMed:7520279, ECO:0000269|PubMed:7628466, ECO:0000269|PubMed:7756982, ECO:0000269|PubMed:9578477, ECO:0000269|PubMed:9694855
source Swiss-Prot : SWS_FT_FI1
37) chain A
residue 42
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:10025942, ECO:0000269|PubMed:10493859, ECO:0000269|PubMed:2553983, ECO:0000269|PubMed:2819062, ECO:0000269|PubMed:3351945, ECO:0000269|PubMed:7520279, ECO:0000269|PubMed:7628466, ECO:0000269|PubMed:7756982, ECO:0000269|PubMed:9578477, ECO:0000269|PubMed:9694855
source Swiss-Prot : SWS_FT_FI1
38) chain A
residue 102
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:10025942, ECO:0000269|PubMed:10493859, ECO:0000269|PubMed:2553983, ECO:0000269|PubMed:2819062, ECO:0000269|PubMed:3351945, ECO:0000269|PubMed:7520279, ECO:0000269|PubMed:7628466, ECO:0000269|PubMed:7756982, ECO:0000269|PubMed:9578477, ECO:0000269|PubMed:9694855
source Swiss-Prot : SWS_FT_FI1
39) chain A
residue 201
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:10025942, ECO:0000269|PubMed:10493859, ECO:0000269|PubMed:2553983, ECO:0000269|PubMed:2819062, ECO:0000269|PubMed:3351945, ECO:0000269|PubMed:7520279, ECO:0000269|PubMed:7628466, ECO:0000269|PubMed:7756982, ECO:0000269|PubMed:9578477, ECO:0000269|PubMed:9694855
source Swiss-Prot : SWS_FT_FI1
40) chain A
residue 212
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:10025942, ECO:0000269|PubMed:10493859, ECO:0000269|PubMed:2553983, ECO:0000269|PubMed:2819062, ECO:0000269|PubMed:3351945, ECO:0000269|PubMed:7520279, ECO:0000269|PubMed:7628466, ECO:0000269|PubMed:7756982, ECO:0000269|PubMed:9578477, ECO:0000269|PubMed:9694855
source Swiss-Prot : SWS_FT_FI1
41) chain A
residue 222
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:10025942, ECO:0000269|PubMed:10493859, ECO:0000269|PubMed:2553983, ECO:0000269|PubMed:2819062, ECO:0000269|PubMed:3351945, ECO:0000269|PubMed:7520279, ECO:0000269|PubMed:7628466, ECO:0000269|PubMed:7756982, ECO:0000269|PubMed:9578477, ECO:0000269|PubMed:9694855
source Swiss-Prot : SWS_FT_FI1
42) chain A
residue 286
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:10025942, ECO:0000269|PubMed:10493859, ECO:0000269|PubMed:2553983, ECO:0000269|PubMed:2819062, ECO:0000269|PubMed:3351945, ECO:0000269|PubMed:7520279, ECO:0000269|PubMed:7628466, ECO:0000269|PubMed:7756982, ECO:0000269|PubMed:9578477, ECO:0000269|PubMed:9694855
source Swiss-Prot : SWS_FT_FI1
43) chain A
residue 293
type BINDING
sequence P
description BINDING => ECO:0000269|PubMed:10025942, ECO:0000269|PubMed:10493859, ECO:0000269|PubMed:2553983, ECO:0000269|PubMed:2819062, ECO:0000269|PubMed:3351945, ECO:0000269|PubMed:7520279, ECO:0000269|PubMed:7628466, ECO:0000269|PubMed:7756982, ECO:0000269|PubMed:9578477, ECO:0000269|PubMed:9694855
source Swiss-Prot : SWS_FT_FI1
44) chain A
residue 201
type SITE
sequence Y
description Important for catalytic activity => ECO:0000250|UniProtKB:P20586
source Swiss-Prot : SWS_FT_FI2
45) chain A
residue 385
type SITE
sequence Y
description Important for catalytic activity => ECO:0000250|UniProtKB:P20586
source Swiss-Prot : SWS_FT_FI2

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