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Structure of PDB 7nbg Chain DDD

Receptor sequence >7nbgDDD (length=310) Species: 9606 (Homo sapiens) [Search protein sequence] QYDISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTG SFKIRGALNAVRSLVRKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQ TAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPA VIAGQGTIALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYA AEPSNADDCYQSKLKGKLMPNLYPPETIADGVKSSIGLNTWPIIRDLVDD IFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSPEVKNI CIVLSGGNVD

3D structure PDB 7nbg Tyrosine 121 moves revealing a ligandable pocket that couples catalysis to ATP-binding in serine racemase. Chain DDD Resolution 1.53 Å 3D structure Catalytic site residues are labeled in the structure [Spin on] [Spin off] [Reset orientation] [High quality] [Low quality] [White background] [Black background] [Download] [Download structure with residue number starting from 1]

Enzymatic activity Catalytic site (original residue number in PDB) K56 S84 E210 A214 D216 G239 L312 S313 Catalytic site (residue number reindexed from 1) K53 S76 E202 A206 D208 G231 L304 S305 Enzyme Commision number 4.3.1.17: L-serine ammonia-lyase. 4.3.1.18: D-serine ammonia-lyase. 5.1.1.18: serine racemase.

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 PLP DDD F55 K56 N86 G185 G186 G187 G188 M189 G239 V240 E283 T285 S313 G314 F52 K53 N78 G177 G178 G179 G180 M181 G231 V232 E275 T277 S305 G306 BS02 CA DDD E210 A214 D216 E202 A206 D208 BS03 OXE DDD S84 Q89 I104 Y121 S76 Q81 I96 Y113 BS04 MG DDD D6 N247 D3 N239

Gene Ontology Molecular Function GO:0000287 magnesium ion binding GO:0003824 catalytic activity GO:0003941 L-serine ammonia-lyase activity GO:0005509 calcium ion binding GO:0005515 protein binding GO:0005524 ATP binding GO:0008721 D-serine ammonia-lyase activity GO:0016594 glycine binding GO:0016829 lyase activity GO:0016853 isomerase activity GO:0018114 threonine racemase activity GO:0030165 PDZ domain binding GO:0030170 pyridoxal phosphate binding GO:0030378 serine racemase activity GO:0042802 identical protein binding GO:0042803 protein homodimerization activity GO:0046872 metal ion binding

	Biological Process
GO:0006520	amino acid metabolic process
GO:0006563	L-serine metabolic process
GO:0009069	serine family amino acid metabolic process
GO:0009410	response to xenobiotic stimulus
GO:0014070	response to organic cyclic compound
GO:0032496	response to lipopolysaccharide
GO:0042866	pyruvate biosynthetic process
GO:0070178	D-serine metabolic process
GO:0070179	D-serine biosynthetic process

	Cellular Component
GO:0005737	cytoplasm
GO:0005829	cytosol
GO:0043025	neuronal cell body
GO:0045177	apical part of cell

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