eF-site ID 1ycb-AB
PDB Code 1ycb
Chain A, B

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Title DISTAL POCKET POLARITY IN LIGAND BINDING TO MYOGLOBIN: DEOXY AND CARBONMONOXY FORMS OF A THREONINE68 (E11) MUTANT INVESTIGATED BY X-RAY CRYSTALLOGRAPHY AND INFRARED SPECTROSCOPY
Classification OXYGEN STORAGE
Compound MYOGLOBIN
Source null (MYG_PIG)
Sequence A:  GLSDGEWQLVLNVWGKVEADVAGHGQEVLIRLFKGHPETL
EKFDKFKHLKSEDEMKASEDLKKHGNTTLTALGGILKKKG
HHEAELTPLAQSHATKHKIPVKYLEFISEAIIQVLQSKHP
GDFGADAQGAMSKALELFRNDMAAKYKELGFQG
B:  GLSDGEWQLVLNVWGKVEADVAGHGQEVLIRLFKGHPETL
EKFDKFKHLKSEDEMKASEDLKKHGNTTLTALGGILKKKG
HHEAELTPLAQSHATKHKIPVKYLEFISEAIIQVLQSKHP
GDFGADAQGAMSKALELFRNDMAAKYKELGFQG
Description


Functional site

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

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

3) chain A
residue 64
type
sequence H
description BINDING SITE FOR RESIDUE HEM A 154
source : AC1

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

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

6) chain A
residue 92
type
sequence S
description BINDING SITE FOR RESIDUE HEM A 154
source : AC1

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

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

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

10) chain A
residue 103
type
sequence Y
description BINDING SITE FOR RESIDUE HEM A 154
source : AC1

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

12) chain B
residue 42
type
sequence K
description BINDING SITE FOR RESIDUE HEM B 154
source : AC2

13) chain B
residue 43
type
sequence F
description BINDING SITE FOR RESIDUE HEM B 154
source : AC2

14) chain B
residue 64
type
sequence H
description BINDING SITE FOR RESIDUE HEM B 154
source : AC2

15) chain B
residue 68
type
sequence T
description BINDING SITE FOR RESIDUE HEM B 154
source : AC2

16) chain B
residue 71
type
sequence A
description BINDING SITE FOR RESIDUE HEM B 154
source : AC2

17) chain B
residue 89
type
sequence L
description BINDING SITE FOR RESIDUE HEM B 154
source : AC2

18) chain B
residue 92
type
sequence S
description BINDING SITE FOR RESIDUE HEM B 154
source : AC2

19) chain B
residue 93
type
sequence H
description BINDING SITE FOR RESIDUE HEM B 154
source : AC2

20) chain B
residue 97
type
sequence H
description BINDING SITE FOR RESIDUE HEM B 154
source : AC2

21) chain B
residue 99
type
sequence I
description BINDING SITE FOR RESIDUE HEM B 154
source : AC2

22) chain B
residue 103
type
sequence Y
description BINDING SITE FOR RESIDUE HEM B 154
source : AC2

23) chain B
residue 138
type
sequence F
description BINDING SITE FOR RESIDUE HEM B 154
source : AC2

24) chain A
residue 65
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:9843395, ECO:0007744|PDB:1MNO
source Swiss-Prot : SWS_FT_FI1

25) chain B
residue 65
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:9843395, ECO:0007744|PDB:1MNO
source Swiss-Prot : SWS_FT_FI1

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

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

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

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

30) chain A
residue 94
type BINDING
sequence A
description proximal binding residue => ECO:0000269|PubMed:2383370, ECO:0000269|PubMed:9843395, ECO:0007744|PDB:1M6C, ECO:0007744|PDB:1M6M, ECO:0007744|PDB:1MDN, ECO:0007744|PDB:1MNH, ECO:0007744|PDB:1MNI, ECO:0007744|PDB:1MNJ, ECO:0007744|PDB:1MNK, ECO:0007744|PDB:1MNO, ECO:0007744|PDB:1MWC, ECO:0007744|PDB:1MWD, ECO:0007744|PDB:1MYG, ECO:0007744|PDB:1MYH, ECO:0007744|PDB:1MYI, ECO:0007744|PDB:1MYJ, ECO:0007744|PDB:1PMB, ECO:0007744|PDB:1YCA, ECO:0007744|PDB:1YCB
source Swiss-Prot : SWS_FT_FI2

31) chain B
residue 94
type BINDING
sequence A
description proximal binding residue => ECO:0000269|PubMed:2383370, ECO:0000269|PubMed:9843395, ECO:0007744|PDB:1M6C, ECO:0007744|PDB:1M6M, ECO:0007744|PDB:1MDN, ECO:0007744|PDB:1MNH, ECO:0007744|PDB:1MNI, ECO:0007744|PDB:1MNJ, ECO:0007744|PDB:1MNK, ECO:0007744|PDB:1MNO, ECO:0007744|PDB:1MWC, ECO:0007744|PDB:1MWD, ECO:0007744|PDB:1MYG, ECO:0007744|PDB:1MYH, ECO:0007744|PDB:1MYI, ECO:0007744|PDB:1MYJ, ECO:0007744|PDB:1PMB, ECO:0007744|PDB:1YCA, ECO:0007744|PDB:1YCB
source Swiss-Prot : SWS_FT_FI2


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