Structure of PDB 5x7q Chain A

Receptor sequence

>5x7qA (length=1247) Species: 1117987 (Paenibacillus sp. 598K)

MAGLGNVTGAVASGDSLTLTLDNGTSASDILELDVLSEELLRVDYRPSGA
APSPSTPMIDPDASWDAVGATIDTSGDPIVVTTPRMRIEIARTPARMTIK
KADGTTLLWEPASGGVFEDGVRFQRGSTDNIYGIRSFNAQEDVGGLLRNS
SDHPAHAGQQGDAGGPFMWSTAGYGVLVDSDGGYPYTDTTGKLEFYYGGT
PTEGRRYTKTNVEYYIMVGEPKEIMASYAQVTGTAPMLPKWSLGFMNFEW
GIDQDELEAHVDGYRARNIPIDAFALDYDWMDYGEDNYGEFRWNTDNFPD
AATTQLKEDMEAEGIRLIGIRKPRIITRDFANQRTQQYYDADSNGYFYPG
HNEYTDYFIPVTVRSFDPYQQASRDWWWQHSIDAFDKGIVGWWNDETDKV
DSGSAQYWFGNFSTGFTSQAMYDGQRDYTNDGVRVWQTARSYYPGAQRYA
TTLWSGDIGTQFYKGELFNWAPGMQEQPRIMLSSANLGQPKWGMDTGGFN
SLGGASGPNPSPELYTRWMQFGAFTPVFRVHGNYNQQRQPWLYGATAEEA
SKAVMHTRYSLLPYMYAYEREASETGLGLIKPLLFDYPNDPQAADYTEAW
MFGDWLLVSPVLGEAQHSKQIYLPAGTWIDYHRGQTYSGGQTIHYPVNAD
TWTDVPLFVKQGAIIPNQQVLDYVDQQSVTTVNVDIFPSASETSFTYYED
DGSSYDYESGSSFEQRLAAQDLSSSVRVEVGAGSGSYTPDVQHYVLKIHG
RAGSAVTAGGSALTGYGDLQALQAASGSGWASGRDIYGDVTYVKLPAASG
SATVVEVSGSAPSAATHAIYEVEDASRSGATPTTRAGINTNHSGYSGSGF
VDKLDVPGAAVTVYANAPVSGDYPVELRYANGSGSAKTLSVYVNAARVQQ
LSLADTGAWSQWGTQTTTLPLTAGQNIITYKYDSDAGDTGGVNLDYIRVP
FAPTQAEYAAESAKLWGGAGTSQDHWFYKGAAFVDNLTGVGAEASFDVYA
PSAGTYNLSLRYANGTGSTKTLSAIVNGGAASTVTLTSPGMNWNLWNEHT
MTATLTAGRNTISFRRNSGNSGNVNLDRLAVSASAITTLASERNLLDNGD
FERDTTYNSNWTQWQPSGQPSAFGIDSGNALHPPEGPARRNQRAYFHSDN
AYQQSIHQVVDVPVNNATYRLEAKVRMKNTTPTTARAEVQGHGGSPIYAN
ISNDGVWKTIVIDNINVTSGSVDVGFYVDSPGYTTLHIDEVTLTRAP

3D structure

• PDB: 5x7q Carbohydrate-binding architecture of the multi-modular alpha-1,6-glucosyltransferase from Paenibacillus sp. 598K, which produces alpha-1,6-glucosyl-alpha-glucosaccharides from starch
• Chain: A
• Resolution: 1.95 Å

Enzymatic activity

• Enzyme Commision number: '2.4.1.-
  3.2.1.20'

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	GLC	A	Y218 G232	Y184 G198
BS02	GLC	A	Y218 Y230	Y184 Y196
BS03	GLC	A	Y220 K226 E228 Y230	Y186 K192 E194 Y196
BS04	GLC	A	Y220 D222 K226	Y186 D188 K192
BS05	GLC	A	K887 D889	K853 D855
BS06	GLC	A	H876 D889 W943 N977	H842 D855 W909 N943
BS07	GLC	A	N1076 W1077	N1042 W1043
BS08	GLC	A	H1009 W1010 N1078 N1142	H975 W976 N1044 N1108
BS09	BGC	A	R362 R368 H1166	R328 R334 H1132
BS10	GLC	A	E1169 H1181 N1213 Y1267 T1269	E1135 H1147 N1179 Y1233 T1235
BS11	GLC	A	D1160 R1177 Y1179 H1271	D1126 R1143 Y1145 H1237
BS12	AC1	A	W1148 S1189 H1191 E1222 Y1261	W1114 S1155 H1157 E1188 Y1227
BS13	CA	A	E855 E857 S880 G883 D979	E821 E823 S846 G849 D945
BS14	CA	A	E995 K1013 A1016 D1111	E961 K979 A982 D1077
BS15	CA	A	D1134 E1136 R1173 Q1176 D1273	D1100 E1102 R1139 Q1142 D1239
BS16	BGC	A	D429 E430 R474 D491 F533 H565	D395 E396 R440 D457 F499 H531
BS17	GLC	A	H1009 N1107 N1109	H975 N1073 N1075
BS18	MG	A	E283 G285	E249 G251
BS19	BGC	A	W284 D311 Y312 K356	W250 D277 Y278 K322

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
• GO:0016787 hydrolase activity
• GO:0030246 carbohydrate binding
• GO:0046872 metal ion binding

Biological Process

• GO:0005975 carbohydrate metabolic process

External links

• PDB: RCSB:5x7q, PDBe:5x7q, PDBj:5x7q
• PDBsum: 5x7q
• PubMed: 28698247
• UniProt: A0A193PKW5