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

click to enlarge
Title Crystal structure of apo heme oxygenase-1
Classification OXIDOREDUCTASE
Compound apo heme oxygenase-1
Source Rattus norvegicus (Rat) (HMOX1_RAT)
Sequence A:  SEFMRNFQKGQVSREGFKLVMASLYHIYTALEEEIERNKQ
NPVYAPLYFPEELHRRAALEQDMAFWYGPHWQEAIPYTPA
TQHYVKRLHEVGGTHPELLVAHAYTRYLGDLSGGQVLKKI
AQKAMALPSSGEGLAFFTFPSIDNPTKFKQLYRARMNTLE
MTPEVKHRVTEEAKTAFLLNIELFEELQALLT
B:  NSEFMRNFQKGQVSREGFKLVMASLYHIYTALEEEIERNK
QNPVYAPLYFPEELHRRAALEQDMAFWYGPHWQEAIPYTP
ATQHYVKRLHEVGGTHPELLVAHAYTRYLGDLSQVLKKIA
QKAMALPSSGEGLAFFTFPSIDNPTKFKQLYRARMNTLEM
TPEVKHRVTEEAKTAFLLNIELFEELQALLTE
C:  NSEFMRNFQKGQVSREGFKLVMASLYHIYTALEEEIERNK
QNPVYAPLYFPEELHRRAALEQDMAFWYGPHWQEAIPYTP
ATQHYVKRLHEVGGTHPELLVAHAYTRYLGDLSGGQVLKK
IAQKAMALPSSGEGLAFFTFPSIDNPTKFKQLYRARMNTL
EMTPEVKHRVTEEAKTAFLLNIELFEELQALLTEEH
Description


Functional site

1) chain C
residue 134
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:P09601
source Swiss-Prot : SWS_FT_FI2

2) chain C
residue 183
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P09601
source Swiss-Prot : SWS_FT_FI2

3) chain A
residue 134
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:P09601
source Swiss-Prot : SWS_FT_FI2

4) chain A
residue 183
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P09601
source Swiss-Prot : SWS_FT_FI2

5) chain B
residue 134
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:P09601
source Swiss-Prot : SWS_FT_FI2

6) chain B
residue 183
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P09601
source Swiss-Prot : SWS_FT_FI2

7) chain C
residue 129-139
type prosite
sequence LVAHAYTRYLG
description HEME_OXYGENASE Heme oxygenase signature. LVAHAYTRYLG
source prosite : PS00593

8) chain C
residue 140
type SITE
sequence D
description Important for catalytic activity => ECO:0000250|UniProtKB:P09601
source Swiss-Prot : SWS_FT_FI4

9) chain A
residue 140
type SITE
sequence D
description Important for catalytic activity => ECO:0000250|UniProtKB:P09601
source Swiss-Prot : SWS_FT_FI4

10) chain B
residue 140
type SITE
sequence D
description Important for catalytic activity => ECO:0000250|UniProtKB:P09601
source Swiss-Prot : SWS_FT_FI4


Display surface

Download
Links