eF-site ID 185l-A
PDB Code 185l
Chain A

click to enlarge
Title SPECIFICITY OF LIGAND BINDING IN A BURIED NON-POLAR CAVITY OF T4 LYSOZYME: LINKAGE OF DYNAMICS AND STRUCTURAL PLASTICITY
Classification HYDROLASE (O-GLYCOSYL)
Compound T4 LYSOZYME
Source Enterobacteria phage T4 (Bacteriophage T4) (LYS_BPT4)
Sequence A:  MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLN
AAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILR
NAKLKPVYDSLDAVRRAAAINMVFQMGETGVAGFTNSLRM
LQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDA
YK
Description


Functional site

1) chain A
residue 78
type
sequence I
description
source : 99A

2) chain A
residue 84
type
sequence L
description
source : 99A

3) chain A
residue 87
type
sequence V
description
source : 99A

4) chain A
residue 88
type
sequence Y
description
source : 99A

5) chain A
residue 99
type
sequence A
description
source : 99A

6) chain A
residue 102
type
sequence M
description
source : 99A

7) chain A
residue 103
type
sequence V
description
source : 99A

8) chain A
residue 109
type
sequence T
description
source : 99A

9) chain A
residue 110
type
sequence G
description
source : 99A

10) chain A
residue 111
type
sequence V
description
source : 99A

11) chain A
residue 112
type
sequence A
description
source : 99A

12) chain A
residue 113
type
sequence G
description
source : 99A

13) chain A
residue 114
type
sequence F
description
source : 99A

14) chain A
residue 118
type
sequence L
description
source : 99A

15) chain A
residue 121
type
sequence L
description
source : 99A

16) chain A
residue 133
type
sequence L
description
source : 99A

17) chain A
residue 153
type
sequence F
description
source : 99A

18) chain A
residue 124
type
sequence K
description BINDING SITE FOR RESIDUE CL A 173
source : AC1

19) chain A
residue 142
type
sequence T
description BINDING SITE FOR RESIDUE CL A 173
source : AC1

20) chain A
residue 144
type
sequence N
description BINDING SITE FOR RESIDUE CL A 173
source : AC1

21) chain A
residue 145
type
sequence R
description BINDING SITE FOR RESIDUE CL A 173
source : AC1

22) chain A
residue 93
type
sequence A
description BINDING SITE FOR RESIDUE HED A 170
source : AC3

23) chain A
residue 100
type
sequence I
description BINDING SITE FOR RESIDUE HED A 170
source : AC3

24) chain A
residue 99
type
sequence A
description BINDING SITE FOR RESIDUE IND A 400
source : AC4

25) chain A
residue 102
type
sequence M
description BINDING SITE FOR RESIDUE IND A 400
source : AC4

26) chain A
residue 111
type
sequence V
description BINDING SITE FOR RESIDUE IND A 400
source : AC4

27) chain A
residue 118
type
sequence L
description BINDING SITE FOR RESIDUE IND A 400
source : AC4

28) chain A
residue 121
type
sequence L
description BINDING SITE FOR RESIDUE IND A 400
source : AC4

29) chain A
residue 153
type
sequence F
description BINDING SITE FOR RESIDUE IND A 400
source : AC4

30) chain A
residue 11
type ACT_SITE
sequence E
description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI1

31) chain A
residue 11
type catalytic
sequence E
description 921
source MCSA : MCSA1

32) chain A
residue 20
type catalytic
sequence D
description 921
source MCSA : MCSA1

33) chain A
residue 20
type ACT_SITE
sequence D
description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI2

34) chain A
residue 32
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI3

35) chain A
residue 104
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI3

36) chain A
residue 117
type BINDING
sequence S
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI4

37) chain A
residue 132
type BINDING
sequence N
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI4


Display surface

Download
Links