eF-site ID 189l-A
PDB Code 189l
Chain A

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Title ENHANCEMENT OF PROTEIN STABILITY BY THE COMBINATION OF POINT MUTATIONS IN T4 LYSOZYME IS ADDITIVE
Classification HYDROLASE (O-GLYCOSYL)
Compound T4 LYSOZYME
Source (LYS_BPT4)
Sequence A:  MNLFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPDLN
VAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILR
NPKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTDSLRM
LQQKRWDEAAANLAKSRWYNQTPDRAKRVITTFRTGTWDA
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 32
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI3

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

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

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

7) 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

8) 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


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