eF-site ID 2d6c-AB
PDB Code 2d6c
Chain A, B

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Title Crystal structure of myoglobin reconstituted with iron porphycene
Classification OXYGEN STORAGE/TRANSPORT
Compound Myoglobin
Source ORGANISM_COMMON: sperm whale; ORGANISM_SCIENTIFIC: Physeter catodon;
Sequence A:  VLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETL
EKFDRFKHLKTEAEMKASEDLKKHGVTVLTALGAILKKKG
HHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHP
GDFGADAQGAMNKALELFRKDIAAKYKELGYQG
B:  VLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETL
EKFDRFKHLKTEAEMKASEDLKKHGVTVLTALGAILKKKG
HHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHP
GDFGADAQGAMNKALELFRKDIAAKYKELGY
Description


Functional site

1) chain A
residue 42
type
sequence K
description BINDING SITE FOR RESIDUE HME A 154
source : AC1

2) chain A
residue 43
type
sequence F
description BINDING SITE FOR RESIDUE HME A 154
source : AC1

3) chain A
residue 45
type
sequence R
description BINDING SITE FOR RESIDUE HME A 154
source : AC1

4) chain A
residue 68
type
sequence V
description BINDING SITE FOR RESIDUE HME A 154
source : AC1

5) chain A
residue 75
type
sequence I
description BINDING SITE FOR RESIDUE HME A 154
source : AC1

6) chain A
residue 89
type
sequence L
description BINDING SITE FOR RESIDUE HME A 154
source : AC1

7) chain A
residue 93
type
sequence H
description BINDING SITE FOR RESIDUE HME A 154
source : AC1

8) chain A
residue 96
type
sequence K
description BINDING SITE FOR RESIDUE HME A 154
source : AC1

9) chain A
residue 97
type
sequence H
description BINDING SITE FOR RESIDUE HME A 154
source : AC1

10) chain A
residue 99
type
sequence I
description BINDING SITE FOR RESIDUE HME A 154
source : AC1

11) chain A
residue 107
type
sequence I
description BINDING SITE FOR RESIDUE HME A 154
source : AC1

12) chain A
residue 138
type
sequence F
description BINDING SITE FOR RESIDUE HME A 154
source : AC1

13) chain A
residue 43
type
sequence F
description BINDING SITE FOR RESIDUE IMD A 155
source : AC2

14) chain A
residue 64
type
sequence H
description BINDING SITE FOR RESIDUE IMD A 155
source : AC2

15) chain A
residue 67
type
sequence T
description BINDING SITE FOR RESIDUE IMD A 155
source : AC2

16) chain A
residue 68
type
sequence V
description BINDING SITE FOR RESIDUE IMD A 155
source : AC2

17) chain B
residue 32
type
sequence L
description BINDING SITE FOR RESIDUE HME B 154
source : AC3

18) chain B
residue 43
type
sequence F
description BINDING SITE FOR RESIDUE HME B 154
source : AC3

19) chain B
residue 68
type
sequence V
description BINDING SITE FOR RESIDUE HME B 154
source : AC3

20) chain B
residue 89
type
sequence L
description BINDING SITE FOR RESIDUE HME B 154
source : AC3

21) chain B
residue 93
type
sequence H
description BINDING SITE FOR RESIDUE HME B 154
source : AC3

22) chain B
residue 96
type
sequence K
description BINDING SITE FOR RESIDUE HME B 154
source : AC3

23) chain B
residue 97
type
sequence H
description BINDING SITE FOR RESIDUE HME B 154
source : AC3

24) chain B
residue 103
type
sequence Y
description BINDING SITE FOR RESIDUE HME B 154
source : AC3

25) chain B
residue 107
type
sequence I
description BINDING SITE FOR RESIDUE HME B 154
source : AC3

26) chain B
residue 43
type
sequence F
description BINDING SITE FOR RESIDUE IMD B 155
source : AC4

27) chain B
residue 64
type
sequence H
description BINDING SITE FOR RESIDUE IMD B 155
source : AC4

28) chain B
residue 67
type
sequence T
description BINDING SITE FOR RESIDUE IMD B 155
source : AC4

29) chain B
residue 68
type
sequence V
description BINDING SITE FOR RESIDUE IMD B 155
source : AC4

30) chain A
residue 65
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:7463482, ECO:0007744|PDB:1MBO
source Swiss-Prot : SWS_FT_FI1

31) chain B
residue 65
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:7463482, ECO:0007744|PDB:1MBO
source Swiss-Prot : SWS_FT_FI1

32) chain A
residue 94
type BINDING
sequence A
description proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:845959, ECO:0007744|PDB:4MBN, ECO:0007744|PDB:5MBN
source Swiss-Prot : SWS_FT_FI2

33) chain B
residue 94
type BINDING
sequence A
description proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:845959, ECO:0007744|PDB:4MBN, ECO:0007744|PDB:5MBN
source Swiss-Prot : SWS_FT_FI2

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

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

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

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


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