eF-site ID 1l44-A
PDB Code 1l44
Chain A

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Title CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY
Classification HYDROLASE (O-GLYCOSYL)
Compound T4 LYSOZYME
Source Enterobacteria phage T4 (Bacteriophage T4) (LYS_BPT4)
Sequence A:  MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLN
AAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILR
NAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLEM
LQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDA
YKNL
Description


Functional site

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

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

3) 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

4) 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

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

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

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

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


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