Structure of PDB 4zas Chain E

Receptor sequence
>4zasE (length=369) Species: 1877 (Micromonospora echinospora) [Search protein sequence]
MIPLSKVAMSPDVSTRVSAVLSSGRLEHGPTVAEYEAAVGSRIGNPRVVS
VNCGTAGLHLALSLAARPGAPGEVLTTPLTFEGTNWPILANGLRIRWVDV
DPATLNMDLDDLAAKISPATRAIVVVHWLGYPVDLNRLRAVVDRATAGYD
RRPLVVEDCAQAWGATYRGAPLGTHGNVCVYSTGAIKILTTGSGGFVVLP
DDDLYDRLRLRRWLGIERASDRITGDYDVAEWGYRFILNEIGGAIGLSNL
ERVDELLRRHRENAAFYDKELAGIDGVEQTERADDREPAFWMYPLKVRDR
PAFMRRLLDAGIATSVVSRRNDAHSCVASARTTLPGLDRVADRVVHIPVG
WWLTEDDRSHVVETIKSGW
3D structure
PDB4zas Structure characterization of sugar aminotransferases CalS13 and WecE provides the basis for a unifying structural model for stereochemical outcome.
ChainE
Resolution2.47 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F96 D173 Q176 G199 K202 Y242 I252
Catalytic site (residue number reindexed from 1) F81 D158 Q161 G184 K187 Y227 I237
Enzyme Commision number ?
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 TYD E G32 R33 L34 E35 R237 G24 R25 L26 E27 R222
Gene Ontology
Molecular Function
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0000271 polysaccharide biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4zas, PDBe:4zas, PDBj:4zas
PDBsum4zas
PubMed
UniProtQ8KND8

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