eF-site/Summary 6b5x-A

eF-site ID	6b5x-A
PDB Code	6b5x
Chain	A

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Title	Beta-Lactamase, unmixed shards crystal form
Classification	HYDROLASE
Compound	Beta-lactamase
Source	(BLAC_MYCTU)

Sequence	A:	DLADRFAELERRYDARLGVYVPATGTTAAIEYRADERFAF CSTFKAPLVAAVLHQNPLTHLDKLITYTSDDIRSISPVAQ QHVQTGMTIGQLCDAAIRYSDGTAANLLLADLGGPGGGTA AFTGYLRSLGDTVSRLDAEEPELNRDPPGDERDTTTPHAI ALVLQQLVLGNALPPDKRALLTDWMARNTTGAKRIRAGFP ADWKVIDKTGTGDYGRANDIAVVWSPTGVPYVVAVMSDRA GGGYDAEPREALLAEAATCVAGVLA

Description

Functional site


1)	chain	A
	residue	70
	type
	sequence	S
	description	binding site for residue PO4 A 301
	source	: AC1

2)	chain	A
	residue	128
	type
	sequence	S
	description	binding site for residue PO4 A 301
	source	: AC1

3)	chain	A
	residue	218
	type
	sequence	T
	description	binding site for residue PO4 A 301
	source	: AC1

4)	chain	A
	residue	237
	type
	sequence	T
	description	binding site for residue PO4 A 301
	source	: AC1

5)	chain	A
	residue	239
	type
	sequence	T
	description	binding site for residue PO4 A 301
	source	: AC1

6)	chain	A
	residue	66-81
	type	prosite
	sequence	FAFCSTFKAPLVAAVL
	description	BETA_LACTAMASE_A Beta-lactamase class-A active site. FaFCSTfKaplVAAVL
	source	prosite : PS00146

7)	chain	A
	residue	70
	type	ACT_SITE
	sequence	S
	description	Acyl-ester intermediate => ECO:0000269\|PubMed:19251630, ECO:0000269\|PubMed:20353175, ECO:0000269\|PubMed:20961112
	source	Swiss-Prot : SWS_FT_FI1

8)	chain	A
	residue	168
	type	ACT_SITE
	sequence	E
	description	Proton acceptor => ECO:0000303\|PubMed:20353175, ECO:0000303\|PubMed:20961112
	source	Swiss-Prot : SWS_FT_FI2

9)	chain	A
	residue	128
	type	BINDING
	sequence	S
	description	BINDING => ECO:0000269\|PubMed:19251630, ECO:0000269\|PubMed:20353175, ECO:0000269\|PubMed:20961112
	source	Swiss-Prot : SWS_FT_FI3

10)	chain	A
	residue	237
	type	BINDING
	sequence	T
	description	BINDING => ECO:0000269\|PubMed:19251630, ECO:0000269\|PubMed:20353175, ECO:0000269\|PubMed:20961112
	source	Swiss-Prot : SWS_FT_FI3

11)	chain	A
	residue	73
	type	SITE
	sequence	K
	description	Increases nucleophilicity of active site Ser => ECO:0000303\|PubMed:20353175, ECO:0000303\|PubMed:20961112
	source	Swiss-Prot : SWS_FT_FI4

12)	chain	A
	residue	103
	type	SITE
	sequence	I
	description	Functions as a gatekeeper residue that regulates substrate accessibility to the enzyme active site => ECO:0000303\|PubMed:24023821
	source	Swiss-Prot : SWS_FT_FI5