Structure of PDB 7aqm Chain B

Receptor sequence

>7aqmB (length=329) Species: 7897 (Latimeria chalumnae)

PMVSLAQVRGALCGALLGDCMGAEFEGSDAVELPDVLEFVRLLEKEKKAG
TLFYTDDTAMTRAVIQSLIAKPDFDEVDMAKRFAEEYKKEPTRGYGAGVV
QVFKKLLSPKYSDVFQPAREQFDGKGSYGNGGAMRVASIALAYPNIQDVI
KFARRSAQLTHASPLGYNGAILQALAVHFALQGELKRDTFLEQLIGEMER
IEGKLPFCSRLKKIKEFLASSNVPKADIVDELGHGIAALESVPTAIYSFL
HCMESDPDIPDLYNNLQRTIIYSISLGGDTDTIATMAGAIAGAYYGMDQV
TPSWKRSCEAIVETEESAVKLYELYCKQL

3D structure

• PDB: 7aqm Mechanistic insights into the three steps of poly(ADP-ribosylation) reversal.
• Chain: B
• Resolution: 2.5 Å

Enzymatic activity

• Enzyme Commision number: 3.2.1.143: poly(ADP-ribose) glycohydrolase.
  3.2.2.-
  3.5.1.-

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	MG	B	T62 D63 D64 D305	T55 D56 D57 D281
BS02	MG	B	E33 D303 D305	E26 D279 D281
BS03	RVK	B	E33 D63 G101 G103 G105 V106 F129 S134 Y135 G136 N137 G138 H168 I260 D303 T306	E26 D56 G94 G96 G98 V99 F122 S127 Y128 G129 N130 G131 H161 I236 D279 T282

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0004649 poly(ADP-ribose) glycohydrolase activity
• GO:0016787 hydrolase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006281 DNA repair
• GO:0060546 negative regulation of necroptotic process
• GO:0140290 peptidyl-serine ADP-deribosylation

Cellular Component

• GO:0005634 nucleus
• GO:0005694 chromosome
• GO:0005737 cytoplasm
• GO:0005739 mitochondrion
• GO:0005759 mitochondrial matrix

External links

• PDB: RCSB:7aqm, PDBe:7aqm, PDBj:7aqm
• PDBsum: 7aqm
• PubMed: 34321462
• UniProt: H3BCW1|ADPRS_LATCH ADP-ribosylhydrolase ARH3 (Gene Name=adprs)