eF-site ID 4tn3-B
PDB Code 4tn3
Chain B

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Title Structure of the BBox-Coiled-coil region of Rhesus Trim5alpha
Classification ANTIVIRAL PROTEIN
Compound TRIM5/cyclophilin A fusion protein/T4 Lysozyme chimera
Source (ENLYS_BPT4)
Sequence B:  PGPEEGQKVDHCARHGEKLLLFCQEDSKVICWLCKDSQEH
RGHHTFLMEEVAQEYHVKLQTALEMLRQKQQEAEKLEADI
REEKASWKIQIDYDKTNVSADFEQLREILDWEESNELQNL
EKEEEDILKSLTKSETEMVQQTQYMRELISELEHRLQGSM
MDLLQGVDGIIKRIENMTLKKPKTFHKNQRRVFRAPDLMN
IFEMLRIDEGLRLKIYKNTEGYYTIGIGHLLTKSPSLNAA
KSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNA
KLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQ
QKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYK
NL
Description


Functional site

1) chain B
residue 108
type
sequence C
description binding site for residue ZN B 700
source : AC3

2) chain B
residue 111
type
sequence D
description binding site for residue ZN B 700
source : AC3

3) chain B
residue 125
type
sequence H
description binding site for residue ZN B 700
source : AC3

4) chain B
residue 128
type
sequence H
description binding site for residue ZN B 700
source : AC3

5) chain B
residue 97
type
sequence C
description binding site for residue ZN B 701
source : AC4

6) chain B
residue 100
type
sequence H
description binding site for residue ZN B 701
source : AC4

7) chain B
residue 116
type
sequence C
description binding site for residue ZN B 701
source : AC4

8) chain B
residue 119
type
sequence C
description binding site for residue ZN B 701
source : AC4

9) chain B
residue 314
type catalytic
sequence E
description 921
source MCSA : MCSA2

10) chain B
residue 323
type catalytic
sequence N
description 921
source MCSA : MCSA2

11) chain B
residue 314
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

12) chain B
residue 323
type ACT_SITE
sequence N
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

13) chain B
residue 335
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI3

14) chain B
residue 407
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI3

15) chain B
residue 420
type BINDING
sequence S
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI4

16) chain B
residue 435
type BINDING
sequence N
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI4


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