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

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Title Structure of chemically modified myoglobin with distal N-tetrazolyl-histidine E7(64)
Classification OXYGEN STORAGE/TRANSPORT
Compound Myoglobin
Source ORGANISM_COMMON: sperm whale; ORGANISM_SCIENTIFIC: Physeter catodon;
Sequence A:  VLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETL
EKFDRFKHLKTEAEMKASEDLKKXGVTVLTALGAILKKKG
HHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHP
GDFGADAQGAMNKALELFRKDIAAKYKELGY
Description


Functional site

1) chain A
residue 51
type
sequence T
description BINDING SITE FOR RESIDUE SO4 A 301
source : AC1

2) chain A
residue 52
type
sequence E
description BINDING SITE FOR RESIDUE SO4 A 301
source : AC1

3) chain A
residue 9
type
sequence L
description BINDING SITE FOR RESIDUE SO4 A 302
source : AC2

4) chain A
residue 124
type
sequence G
description BINDING SITE FOR RESIDUE SO4 A 302
source : AC2

5) chain A
residue 125
type
sequence A
description BINDING SITE FOR RESIDUE SO4 A 302
source : AC2

6) chain A
residue 126
type
sequence D
description BINDING SITE FOR RESIDUE SO4 A 302
source : AC2

7) chain A
residue 127
type
sequence A
description BINDING SITE FOR RESIDUE SO4 A 302
source : AC2

8) chain A
residue 39
type
sequence T
description BINDING SITE FOR RESIDUE HEM A 154
source : AC3

9) chain A
residue 42
type
sequence K
description BINDING SITE FOR RESIDUE HEM A 154
source : AC3

10) chain A
residue 43
type
sequence F
description BINDING SITE FOR RESIDUE HEM A 154
source : AC3

11) chain A
residue 45
type
sequence R
description BINDING SITE FOR RESIDUE HEM A 154
source : AC3

12) chain A
residue 64
type
sequence X
description BINDING SITE FOR RESIDUE HEM A 154
source : AC3

13) chain A
residue 68
type
sequence V
description BINDING SITE FOR RESIDUE HEM A 154
source : AC3

14) chain A
residue 71
type
sequence A
description BINDING SITE FOR RESIDUE HEM A 154
source : AC3

15) chain A
residue 89
type
sequence L
description BINDING SITE FOR RESIDUE HEM A 154
source : AC3

16) chain A
residue 92
type
sequence S
description BINDING SITE FOR RESIDUE HEM A 154
source : AC3

17) chain A
residue 93
type
sequence H
description BINDING SITE FOR RESIDUE HEM A 154
source : AC3

18) chain A
residue 97
type
sequence H
description BINDING SITE FOR RESIDUE HEM A 154
source : AC3

19) chain A
residue 99
type
sequence I
description BINDING SITE FOR RESIDUE HEM A 154
source : AC3

20) chain A
residue 103
type
sequence Y
description BINDING SITE FOR RESIDUE HEM A 154
source : AC3

21) chain A
residue 120
type
sequence P
description BINDING SITE FOR RESIDUE HEM A 154
source : AC3

22) chain A
residue 121
type
sequence G
description BINDING SITE FOR RESIDUE HEM A 154
source : AC3

23) chain A
residue 138
type
sequence F
description BINDING SITE FOR RESIDUE HEM A 154
source : AC3

24) chain A
residue 68
type MOD_RES
sequence V
description Phosphothreonine => ECO:0000250|UniProtKB:P04247
source Swiss-Prot : SWS_FT_FI4

25) chain A
residue 4
type MOD_RES
sequence E
description Phosphoserine => ECO:0000250|UniProtKB:Q9QZ76
source Swiss-Prot : SWS_FT_FI3

26) chain A
residue 65
type BINDING
sequence G
description distal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:845959
source Swiss-Prot : SWS_FT_FI1

27) chain A
residue 94
type BINDING
sequence A
description proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:845959
source Swiss-Prot : SWS_FT_FI2


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