Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1UKO

Crystal structure of soybean beta-amylase mutant substituted at surface region

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000272	biological_process	polysaccharide catabolic process
A	0008152	biological_process	metabolic process
A	0016161	molecular_function	beta-amylase activity
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0102229	molecular_function	amylopectin maltohydrolase activity
B	0000272	biological_process	polysaccharide catabolic process
B	0008152	biological_process	metabolic process
B	0016161	molecular_function	beta-amylase activity
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0102229	molecular_function	amylopectin maltohydrolase activity
C	0000272	biological_process	polysaccharide catabolic process
C	0008152	biological_process	metabolic process
C	0016161	molecular_function	beta-amylase activity
C	0016787	molecular_function	hydrolase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0102229	molecular_function	amylopectin maltohydrolase activity
D	0000272	biological_process	polysaccharide catabolic process
D	0008152	biological_process	metabolic process
D	0016161	molecular_function	beta-amylase activity
D	0016787	molecular_function	hydrolase activity
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0102229	molecular_function	amylopectin maltohydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 3000

Chain	Residue
A	TYR67
A	SER160
A	ASN164
A	HOH1773

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 3001

Chain	Residue
A	ARG347
A	SER349
A	HOH701
A	HOH1822

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 3002

Chain	Residue
A	ARG376
A	HOH1871
A	HIS336

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 3003

Chain	Residue
A	LYS291
A	ARG376
A	PHE414
A	ASN455
A	HIS456
A	ALA457

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 3004

Chain	Residue
B	TYR67
B	SER160
B	ASN164
B	HOH1959

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 3005

Chain	Residue
B	ARG347
B	SER349
B	HOH1722
B	HOH1726

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 3006

Chain	Residue
B	HIS336
B	ARG376
B	HOH1173
B	HOH1180

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 B 3007

Chain	Residue
B	LYS291
B	ARG376
B	PHE414
B	ASN455
B	HIS456
B	ALA457
B	HOH1325
B	HOH1704

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 3008

Chain	Residue
C	TYR67
C	SER160
C	ASN164
C	HOH1205
C	HOH1530

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 3009

Chain	Residue
C	ARG347
C	SER349
C	HOH1266
C	HOH1588

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 3010

Chain	Residue
C	HIS336
C	ARG376
C	HOH1263
C	HOH1584

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 3011

Chain	Residue
C	LYS291
C	ARG376
C	PHE414
C	ASN455
C	ALA457

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 3012

Chain	Residue
D	TYR67
D	SER160
D	ASN164
D	HOH1318

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 3013

Chain	Residue
D	ARG347
D	SER349
D	HOH971

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 3014

Chain	Residue
D	HIS336
D	ARG376
D	HOH969
D	HOH1346

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 3015

Chain	Residue
B	HOH1154
D	LYS291
D	ARG376
D	PHE414
D	ASN455
D	ALA457

site_id	BC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO4 A 3016

Chain	Residue
A	ARG70

site_id	BC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO4 B 3017

Chain	Residue
B	ARG70

site_id	CC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO4 C 3018

Chain	Residue
C	ARG70

site_id	CC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO4 D 3019

Chain	Residue
D	ARG70

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 3020

Chain	Residue
A	ASN98
A	PRO193
A	GLN194
A	HOH675
A	HOH1794
A	HOH1855

site_id	CC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 B 3021

Chain	Residue
B	ASN98
B	TYR192
B	PRO193
B	GLN194
B	HOH1148
B	HOH1638
B	HOH1639
B	HOH1656

site_id	CC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 3022

Chain	Residue
C	ASN98
C	PRO193
C	GLN194
C	HOH1405
C	HOH1406
C	HOH1407

site_id	CC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 3023

Chain	Residue
D	HOH1298
D	HOH1307
D	HOH1319
D	ASN98
D	PRO193
D	GLN194

Functional Information from PROSITE/UniProt

site_id	PS00506
Number of Residues	9
Details	BETA_AMYLASE_1 Beta-amylase active site 1. HqCGGNVGD

Chain	Residue	Details
A	HIS93-ASP101

site_id	PS00679
Number of Residues	11
Details	BETA_AMYLASE_2 Beta-amylase active site 2. GpAGELRYPSY

Chain	Residue	Details
A	GLY182-TYR192

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000255\|PROSITE-ProRule:PRU10050, ECO:0000269\|PubMed:15178253, ECO:0000269\|PubMed:2474529, ECO:0000269\|PubMed:8011643, ECO:0000269\|PubMed:8174545

Chain	Residue	Details
A	LEU187
B	LEU187
C	LEU187
D	LEU187

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000269\|PubMed:15178253, ECO:0000269\|PubMed:8011643

Chain	Residue	Details
A	ASN381
B	ASN381
C	ASN381
D	ASN381

site_id	SWS_FT_FI3
Number of Residues	32
Details	BINDING: BINDING => ECO:0000269\|PubMed:15178253

Chain	Residue	Details
A	VAL54
B	GLN94
B	ILE102
B	VAL296
B	TRP301
B	CYS343
B	ALA382
B	LEU421
C	VAL54
C	GLN94
C	ILE102
A	GLN94
C	VAL296
C	TRP301
C	CYS343
C	ALA382
C	LEU421
D	VAL54
D	GLN94
D	ILE102
D	VAL296
D	TRP301
A	ILE102
D	CYS343
D	ALA382
D	LEU421
A	VAL296
A	TRP301
A	CYS343
A	ALA382
A	LEU421
B	VAL54

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: N-acetylalanine => ECO:0000269\|PubMed:2430952

Chain	Residue	Details
A	THR2
B	THR2
C	THR2
D	THR2

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 436

Chain	Residue	Details
A	ILE102	electrostatic stabiliser
A	LEU187	proton shuttle (general acid/base)
A	CYS343	electrostatic stabiliser
A	ASN381	proton shuttle (general acid/base)
A	PRO384	steric role

site_id	MCSA2
Number of Residues	5
Details	M-CSA 436

Chain	Residue	Details
B	ILE102	electrostatic stabiliser
B	LEU187	proton shuttle (general acid/base)
B	CYS343	electrostatic stabiliser
B	ASN381	proton shuttle (general acid/base)
B	PRO384	steric role

site_id	MCSA3
Number of Residues	5
Details	M-CSA 436

Chain	Residue	Details
C	ILE102	electrostatic stabiliser
C	LEU187	proton shuttle (general acid/base)
C	CYS343	electrostatic stabiliser
C	ASN381	proton shuttle (general acid/base)
C	PRO384	steric role

site_id	MCSA4
Number of Residues	5
Details	M-CSA 436

Chain	Residue	Details
D	ILE102	electrostatic stabiliser
D	LEU187	proton shuttle (general acid/base)
D	CYS343	electrostatic stabiliser
D	ASN381	proton shuttle (general acid/base)
D	PRO384	steric role

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)