eF-site ID 1c6d-A
PDB Code 1c6d
Chain A

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Title T4 LYSOZYME MUTANT C54T/C97A/L99A IN THE PRESENCE OF 16 ATM KRYPTON
Classification HYDROLASE
Compound PROTEIN (LYSOZYME)
Source Enterobacteria phage T4 (Bacteriophage T4) (LYS_BPT4)
Sequence A:  MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLN
AAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILR
NAKLKPVYDSLDAVRRAAAINMVFQMGETGVAGFTNSLRM
LQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDA
YK
Description


Functional site

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

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

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

4) chain A
residue 49
type
sequence A
description BINDING SITE FOR RESIDUE CL A 178
source : AC2

5) chain A
residue 99
type
sequence A
description BINDING SITE FOR RESIDUE KR A 500
source : AC3

6) chain A
residue 118
type
sequence L
description BINDING SITE FOR RESIDUE KR A 501
source : AC4

7) chain A
residue 111
type
sequence V
description BINDING SITE FOR RESIDUE KR A 502
source : AC5

8) chain A
residue 118
type
sequence L
description BINDING SITE FOR RESIDUE KR A 502
source : AC5

9) chain A
residue 72
type
sequence D
description BINDING SITE FOR RESIDUE BME A 901
source : AC6

10) chain A
residue 72
type
sequence D
description BINDING SITE FOR RESIDUE BME A 901
source : AC6

11) chain A
residue 68
type
sequence N
description BINDING SITE FOR RESIDUE BME A 902
source : AC7

12) chain A
residue 72
type
sequence D
description BINDING SITE FOR RESIDUE BME A 902
source : AC7

13) chain A
residue 93
type
sequence A
description BINDING SITE FOR RESIDUE BME A 902
source : AC7

14) 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

15) 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

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

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

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

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

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

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


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