eF-site ID 1qf7-D
PDB Code 1qf7
Chain D

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Title STRUCTURE OF THE MUTANT HIS392GLN OF CATALASE HPII FROM E. COLI
Classification OXIDOREDUCTASE
Compound PROTEIN (CATALASE HPII)
Source (CATE_ECOLI)
Sequence D:  DSLAPEDGSHRPAAEPTPPGAQPTAPGSLKAPDTRNEKLN
SLEDVRKGSENYALTTNQGVRIADDQNSLRAGSRGPTLLE
DFILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLSD
ITKADFLSDPNKITPVFVRFSTVQGGAGSADTVRDIRGFA
TKFYTEEGIFDLVGNNTPIFFIQDAHKFPDFVHAVKPEPH
WAIPQGQSAHDTFWDYVSLQPETLHNVMWAMSDRGIPRSY
RTMEGFGIHTFRLINAEGKATFVRFHWKPLAGKASLVWDE
AQKLTGRDPDFHRRELWEAIEAGDFPEYELGFQLIPEEDE
FKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAEN
EQAAFQPGHIVPGLDFTNDPLLQGRLFSYTDTQISRLGGP
NFHEIPINRPTCPYHNFQRDGMHRMGIDTNPANYEPNSIN
DNWPRETPPGPKRGGFESYQERVEGNKVRERSPSFGEYYS
HPRLFWLSQTPFEQRHIVDGFSFELSKVVRPYIRERVVDQ
LAHIDLTLAQAVAKNLGIELTDDQLNITPPPDVNGLKKDP
SLSLYAIPDGDVKGRVVAILLNDEVRSADLLAILKALKAK
GVHAKLLYSRMGEVTADDGTVLPIAATFAGAPSLTVDAVI
VPCGNIADIADNGDANYYLMEAYKHLKPIALAGDARKFKA
TIKIADQGEEGIVEADSADGSFMDELLTLMAAHRVWSRIP
KIDKIPA
Description


Functional site

1) chain D
residue 128
type
sequence H
description ESSENTIAL CATALYTIC RESIDUES.
source : CAD

2) chain D
residue 201
type
sequence N
description ESSENTIAL CATALYTIC RESIDUES.
source : CAD

3) chain D
residue 415
type
sequence Y
description ESSENTIAL CATALYTIC RESIDUES.
source : CAD

4) chain D
residue 125
type
sequence R
description BINDING SITE FOR RESIDUE HEM D 754
source : AC4

5) chain D
residue 126
type
sequence I
description BINDING SITE FOR RESIDUE HEM D 754
source : AC4

6) chain D
residue 127
type
sequence V
description BINDING SITE FOR RESIDUE HEM D 754
source : AC4

7) chain D
residue 128
type
sequence H
description BINDING SITE FOR RESIDUE HEM D 754
source : AC4

8) chain D
residue 165
type
sequence R
description BINDING SITE FOR RESIDUE HEM D 754
source : AC4

9) chain D
residue 184
type
sequence G
description BINDING SITE FOR RESIDUE HEM D 754
source : AC4

10) chain D
residue 199
type
sequence V
description BINDING SITE FOR RESIDUE HEM D 754
source : AC4

11) chain D
residue 200
type
sequence G
description BINDING SITE FOR RESIDUE HEM D 754
source : AC4

12) chain D
residue 201
type
sequence N
description BINDING SITE FOR RESIDUE HEM D 754
source : AC4

13) chain D
residue 214
type
sequence F
description BINDING SITE FOR RESIDUE HEM D 754
source : AC4

14) chain D
residue 274
type
sequence I
description BINDING SITE FOR RESIDUE HEM D 754
source : AC4

15) chain D
residue 275
type
sequence H
description BINDING SITE FOR RESIDUE HEM D 754
source : AC4

16) chain D
residue 391
type
sequence F
description BINDING SITE FOR RESIDUE HEM D 754
source : AC4

17) chain D
residue 407
type
sequence L
description BINDING SITE FOR RESIDUE HEM D 754
source : AC4

18) chain D
residue 411
type
sequence R
description BINDING SITE FOR RESIDUE HEM D 754
source : AC4

19) chain D
residue 414
type
sequence S
description BINDING SITE FOR RESIDUE HEM D 754
source : AC4

20) chain D
residue 415
type
sequence Y
description BINDING SITE FOR RESIDUE HEM D 754
source : AC4

21) chain D
residue 418
type
sequence T
description BINDING SITE FOR RESIDUE HEM D 754
source : AC4

22) chain D
residue 419
type
sequence Q
description BINDING SITE FOR RESIDUE HEM D 754
source : AC4

23) chain D
residue 422
type
sequence R
description BINDING SITE FOR RESIDUE HEM D 754
source : AC4

24) chain D
residue 128
type catalytic
sequence H
description 573
source MCSA : MCSA4

25) chain D
residue 201
type catalytic
sequence N
description 573
source MCSA : MCSA4

26) chain D
residue 392
type catalytic
sequence Q
description 573
source MCSA : MCSA4

27) chain D
residue 415
type BINDING
sequence Y
description axial binding residue
source Swiss-Prot : SWS_FT_FI2

28) chain D
residue 392
type CROSSLNK
sequence Q
description 3'-histidyl-3-tyrosine (His-Tyr)
source Swiss-Prot : SWS_FT_FI3

29) chain D
residue 415
type CROSSLNK
sequence Y
description 3'-histidyl-3-tyrosine (His-Tyr)
source Swiss-Prot : SWS_FT_FI3

30) chain D
residue 128
type ACT_SITE
sequence H
description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013
source Swiss-Prot : SWS_FT_FI1

31) chain D
residue 201
type ACT_SITE
sequence N
description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10013
source Swiss-Prot : SWS_FT_FI1


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