eF-site ID 1mz0_2-A
PDB Code 1mz0
Model 2
Chain A

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Title STRUCTURE OF MYOGLOBIN MB-YQR 316 ns AFTER PHOTOLYSIS OF CARBON MONOXIDE SOLVED FROM LAUE DATA AT RT.
Classification OXYGEN STORAGE/TRANSPORT
Compound Myoglobin
Source (MYG_PHYCA)
Sequence A:  MVLSEGEWQLVLHVWAKVEADVAGHGQDIYIRLFKSHPET
LEKFDRFKHLKTEAEMKASEDLKKQGVRVLTALGAILKKK
GHHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRH
PGNFGADAQGAMNKALELFRKDIAAKYKELGYQG
Description


Functional site

1) chain A
residue 16
type
sequence K
description BINDING SITE FOR RESIDUE SO4 A 501
source : AC1

2) chain A
residue 3
type
sequence S
description BINDING SITE FOR RESIDUE SO4 A 504
source : AC2

3) chain A
residue 4
type
sequence E
description BINDING SITE FOR RESIDUE SO4 A 504
source : AC2

4) chain A
residue 51
type
sequence T
description BINDING SITE FOR RESIDUE SO4 A 504
source : AC2

5) chain A
residue 52
type
sequence E
description BINDING SITE FOR RESIDUE SO4 A 504
source : AC2

6) chain A
residue 53
type
sequence A
description BINDING SITE FOR RESIDUE SO4 A 504
source : AC2

7) chain A
residue 39
type
sequence T
description BINDING SITE FOR RESIDUE HEM A 200
source : AC3

8) chain A
residue 42
type
sequence K
description BINDING SITE FOR RESIDUE HEM A 200
source : AC3

9) chain A
residue 43
type
sequence F
description BINDING SITE FOR RESIDUE HEM A 200
source : AC3

10) chain A
residue 45
type
sequence R
description BINDING SITE FOR RESIDUE HEM A 200
source : AC3

11) chain A
residue 64
type
sequence Q
description BINDING SITE FOR RESIDUE HEM A 200
source : AC3

12) chain A
residue 89
type
sequence L
description BINDING SITE FOR RESIDUE HEM A 200
source : AC3

13) chain A
residue 92
type
sequence S
description BINDING SITE FOR RESIDUE HEM A 200
source : AC3

14) chain A
residue 93
type
sequence H
description BINDING SITE FOR RESIDUE HEM A 200
source : AC3

15) chain A
residue 97
type
sequence H
description BINDING SITE FOR RESIDUE HEM A 200
source : AC3

16) chain A
residue 99
type
sequence I
description BINDING SITE FOR RESIDUE HEM A 200
source : AC3

17) chain A
residue 103
type
sequence Y
description BINDING SITE FOR RESIDUE HEM A 200
source : AC3

18) chain A
residue 29
type
sequence Y
description BINDING SITE FOR RESIDUE CMO A 201
source : AC4

19) chain A
residue 43
type
sequence F
description BINDING SITE FOR RESIDUE CMO A 201
source : AC4

20) chain A
residue 68
type
sequence V
description BINDING SITE FOR RESIDUE CMO A 201
source : AC4

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

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

23) 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

24) 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


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