eF-site ID 172l-A
PDB Code 172l
Chain A

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Title PROTEIN FLEXIBILITY AND ADAPTABILITY SEEN IN 25 CRYSTAL FORMS OF T4 LYSOZYME
Classification HYDROLASE (O-GLYCOSYL)
Compound T4 LYSOZYME
Source Enterobacteria phage T4 (Bacteriophage T4) (LYS_BPT4)
Sequence A:  MNCFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLN
AAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILR
NAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRM
LQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDA
YKNL
Description (1)  LYSOZYME (E.C.3.2.1.17) MUTANT WITH ILE 3 REPLACED BY CYS (I3C)


Functional site

1) chain A
residue 6
type
sequence M
description COMPRISES RESIDUES WITHIN 8 ANGSTROMS OF ATOM SG CYS 3
source : I3C

2) chain A
residue 7
type
sequence L
description COMPRISES RESIDUES WITHIN 8 ANGSTROMS OF ATOM SG CYS 3
source : I3C

3) chain A
residue 67
type
sequence F
description COMPRISES RESIDUES WITHIN 8 ANGSTROMS OF ATOM SG CYS 3
source : I3C

4) chain A
residue 71
type
sequence V
description COMPRISES RESIDUES WITHIN 8 ANGSTROMS OF ATOM SG CYS 3
source : I3C

5) chain A
residue 94
type
sequence V
description COMPRISES RESIDUES WITHIN 8 ANGSTROMS OF ATOM SG CYS 3
source : I3C

6) chain A
residue 96
type
sequence R
description COMPRISES RESIDUES WITHIN 8 ANGSTROMS OF ATOM SG CYS 3
source : I3C

7) chain A
residue 97
type
sequence C
description COMPRISES RESIDUES WITHIN 8 ANGSTROMS OF ATOM SG CYS 3
source : I3C

8) chain A
residue 100
type
sequence I
description COMPRISES RESIDUES WITHIN 8 ANGSTROMS OF ATOM SG CYS 3
source : I3C

9) chain A
residue 101
type
sequence N
description COMPRISES RESIDUES WITHIN 8 ANGSTROMS OF ATOM SG CYS 3
source : I3C

10) chain A
residue 158
type
sequence W
description COMPRISES RESIDUES WITHIN 8 ANGSTROMS OF ATOM SG CYS 3
source : I3C

11) chain A
residue 50
type
sequence I
description BINDING SITE FOR RESIDUE BME A 170
source : AC1

12) chain A
residue 52
type
sequence R
description BINDING SITE FOR RESIDUE BME A 170
source : AC1

13) chain A
residue 53
type
sequence N
description BINDING SITE FOR RESIDUE BME A 170
source : AC1

14) chain A
residue 54
type
sequence C
description BINDING SITE FOR RESIDUE BME A 170
source : AC1

15) chain A
residue 57
type
sequence V
description BINDING SITE FOR RESIDUE BME A 170
source : AC1

16) chain A
residue 58
type
sequence I
description BINDING SITE FOR RESIDUE BME A 170
source : AC1

17) chain A
residue 59
type
sequence T
description BINDING SITE FOR RESIDUE BME A 170
source : AC1

18) chain A
residue 62
type
sequence E
description BINDING SITE FOR RESIDUE BME A 170
source : AC1

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

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

21) 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

22) 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

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

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

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

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


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