eF-site ID 2cyp-A
PDB Code 2cyp
Chain A

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Title Crystal structure of yeast cytochrome C peroxidase refined at 1.7-angstroms resolution
Classification OXIDOREDUCTASE (H2O2(A))
Compound CYTOCHROME C PEROXIDASE
Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (CCPR_YEAST)
Sequence A:  TPLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIG
YGPVLVRLAWHTSGTWDKHDNTGGSYGGTYRFKKEFNDPS
NAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQG
PKIPWRCGRVDTPEDTTPDNGRLPDADKDADYVRTFFQRL
NMNDREVVALMGAHALGKTHLKNSGYEGPWGAANNVFTNE
FYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQD
PKYLSIVKEYANDQDKFFKDFSKAFEKLLENGITFPKDAP
SPFIFKTLEEQGL
Description


Functional site

1) chain A
residue 44
type
sequence P
description BINDING SITE FOR RESIDUE HEM A 295
source : AC1

2) chain A
residue 48
type
sequence R
description BINDING SITE FOR RESIDUE HEM A 295
source : AC1

3) chain A
residue 51
type
sequence W
description BINDING SITE FOR RESIDUE HEM A 295
source : AC1

4) chain A
residue 145
type
sequence P
description BINDING SITE FOR RESIDUE HEM A 295
source : AC1

5) chain A
residue 146
type
sequence D
description BINDING SITE FOR RESIDUE HEM A 295
source : AC1

6) chain A
residue 172
type
sequence M
description BINDING SITE FOR RESIDUE HEM A 295
source : AC1

7) chain A
residue 174
type
sequence A
description BINDING SITE FOR RESIDUE HEM A 295
source : AC1

8) chain A
residue 175
type
sequence H
description BINDING SITE FOR RESIDUE HEM A 295
source : AC1

9) chain A
residue 177
type
sequence L
description BINDING SITE FOR RESIDUE HEM A 295
source : AC1

10) chain A
residue 178
type
sequence G
description BINDING SITE FOR RESIDUE HEM A 295
source : AC1

11) chain A
residue 179
type
sequence K
description BINDING SITE FOR RESIDUE HEM A 295
source : AC1

12) chain A
residue 180
type
sequence T
description BINDING SITE FOR RESIDUE HEM A 295
source : AC1

13) chain A
residue 181
type
sequence H
description BINDING SITE FOR RESIDUE HEM A 295
source : AC1

14) chain A
residue 184
type
sequence N
description BINDING SITE FOR RESIDUE HEM A 295
source : AC1

15) chain A
residue 185
type
sequence S
description BINDING SITE FOR RESIDUE HEM A 295
source : AC1

16) chain A
residue 191
type
sequence W
description BINDING SITE FOR RESIDUE HEM A 295
source : AC1

17) chain A
residue 232
type
sequence L
description BINDING SITE FOR RESIDUE HEM A 295
source : AC1

18) chain A
residue 48
type
sequence R
description BINDING SITE FOR RESIDUE O A 296
source : AC2

19) chain A
residue 51
type
sequence W
description BINDING SITE FOR RESIDUE O A 296
source : AC2

20) chain A
residue 52
type
sequence H
description BINDING SITE FOR RESIDUE O A 296
source : AC2

21) chain A
residue 48
type catalytic
sequence R
description 709
source MCSA : MCSA1

22) chain A
residue 52
type catalytic
sequence H
description 709
source MCSA : MCSA1

23) chain A
residue 191
type catalytic
sequence W
description 709
source MCSA : MCSA1

24) chain A
residue 52
type ACT_SITE
sequence H
description Proton acceptor
source Swiss-Prot : SWS_FT_FI1

25) chain A
residue 191
type ACT_SITE
sequence W
description Tryptophan radical intermediate
source Swiss-Prot : SWS_FT_FI2

26) chain A
residue 48
type SITE
sequence R
description Transition state stabilizer
source Swiss-Prot : SWS_FT_FI4

27) chain A
residue 167-177
type prosite
sequence EVVALMGAHAL
description PEROXIDASE_1 Peroxidases proximal heme-ligand signature. EVVALMGAHAL
source prosite : PS00435

28) chain A
residue 43-54
type prosite
sequence GPVLVRLAWHTS
description PEROXIDASE_2 Peroxidases active site signature. GPvlVRLaWHTS
source prosite : PS00436

29) chain A
residue 153
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI5

30) chain A
residue 175
type BINDING
sequence H
description axial binding residue
source Swiss-Prot : SWS_FT_FI3


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