eF-site ID 216l-A
PDB Code 216l
Chain A

click to enlarge
Title STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME
Classification HYDROLASE(O-GLYCOSYL)
Compound T4 LYSOZYME
Source Enterobacteria phage T4 (Bacteriophage T4) (LYS_BPT4)
Sequence A:  MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLN
AAKWELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILR
NAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRM
LQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDA
YK
Description (1)  LYSOZYME (E.C.3.2.1.17) MUTANT WITH SER 44 REPLACED BY TRP, CYS 54 REPLACED BY THR, CYS 97 REPLACED BY ALA (S44W, C54T, C97A)


Functional site

1) chain A
residue 11
type ACT_SITE
ligand
sequence E
description Proton donor. {ECO:0000255|HAMAP- Rule:MF_04110, ECO:0000269|PubMed:3382407}.
source Swiss-Prot : SWS_FT_FI1

2) chain A
residue 20
type ACT_SITE
ligand
sequence D
description Nucleophile. {ECO:0000255|HAMAP- Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407}.
source Swiss-Prot : SWS_FT_FI2

3) chain A
residue 32
type BINDING
ligand
sequence L
description N-acetyl-D-glucosamine; via amide nitrogen. {ECO:0000255|HAMAP- Rule:MF_04110, ECO:0000269|PubMed:8266098}.
source Swiss-Prot : SWS_FT_FI3

4) chain A
residue 104
type BINDING
ligand
sequence F
description N-acetyl-D-glucosamine; via amide nitrogen. {ECO:0000255|HAMAP- Rule:MF_04110, ECO:0000269|PubMed:8266098}.
source Swiss-Prot : SWS_FT_FI3

5) chain A
residue 117
type SITE
ligand
sequence S
description Substrate-binding. {ECO:0000303|PubMed:7831309}.
source Swiss-Prot : SWS_FT_FI4

6) chain A
residue 132
type SITE
ligand
sequence N
description Substrate-binding. {ECO:0000303|PubMed:7831309}.
source Swiss-Prot : SWS_FT_FI4

7) chain A
residue 11
type catalytic
ligand
sequence E
description Annotated By Reference To The Literature 206l
source CSA : CSA1

8) chain A
residue 20
type catalytic
ligand
sequence D
description Annotated By Reference To The Literature 206l
source CSA : CSA1


Display surface

Download
Links