eF-site ID 2blj-M
PDB Code 2blj
Chain M

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Title Structure of L29W MbCO
Classification OXYGEN TRANSPORT
Compound MYOGLOBIN
Source (MYG_PHYCA)
Sequence M:  VLSEGEWQLVLHVWAKVEADVAGHGQDIWIRLFKSHPETL
EKFDRFKHLKTEAEMKASEDLKKHGVTVLTALGAILKKKG
HHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHP
GNFGADAQGAMNKALELFRKDIAAKYKELGYQG
Description (1)  MYOGLOBIN


Functional site

1) chain M
residue 42
type
sequence K
description BINDING SITE FOR RESIDUE HEM M1154
source : AC1

2) chain M
residue 43
type
sequence F
description BINDING SITE FOR RESIDUE HEM M1154
source : AC1

3) chain M
residue 45
type
sequence R
description BINDING SITE FOR RESIDUE HEM M1154
source : AC1

4) chain M
residue 89
type
sequence L
description BINDING SITE FOR RESIDUE HEM M1154
source : AC1

5) chain M
residue 92
type
sequence S
description BINDING SITE FOR RESIDUE HEM M1154
source : AC1

6) chain M
residue 93
type
sequence H
description BINDING SITE FOR RESIDUE HEM M1154
source : AC1

7) chain M
residue 97
type
sequence H
description BINDING SITE FOR RESIDUE HEM M1154
source : AC1

8) chain M
residue 99
type
sequence I
description BINDING SITE FOR RESIDUE HEM M1154
source : AC1

9) chain M
residue 103
type
sequence Y
description BINDING SITE FOR RESIDUE HEM M1154
source : AC1

10) chain M
residue 29
type
sequence W
description BINDING SITE FOR RESIDUE CMO M1155
source : AC2

11) chain M
residue 43
type
sequence F
description BINDING SITE FOR RESIDUE CMO M1155
source : AC2

12) chain M
residue 64
type
sequence H
description BINDING SITE FOR RESIDUE CMO M1155
source : AC2

13) chain M
residue 68
type
sequence V
description BINDING SITE FOR RESIDUE CMO M1155
source : AC2

14) chain M
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

15) chain M
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

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

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


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