Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6X25

CRYSTAL STRUCTURE OF INOSITOL POLYPHOSPHATE 1-PHOSPHATASE INPP1 IN COMPLEX GADOLINIUM AFTER ADDITION OF INOSITOL 1,3,4-TRISPHOSPHATE AND LITHIUM AT 3.2 ANGSTROM RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0004441molecular_functioninositol-1,4-bisphosphate 1-phosphatase activity
A0016787molecular_functionhydrolase activity
A0046854biological_processphosphatidylinositol phosphate biosynthetic process
A0046872molecular_functionmetal ion binding
A0052829molecular_functioninositol-1,3,4-trisphosphate 1-phosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue GD A 501
ChainResidue
AASP54
AGLU79
AASP153
AILE155
ASO4504

site_idAC2
Number of Residues5
Detailsbinding site for residue GD A 502
ChainResidue
ASO4504
AGLU79
AASP153
AASP156
AASP317

site_idAC3
Number of Residues8
Detailsbinding site for residue SO4 A 503
ChainResidue
ASER268
AGLU269
AALA288
AALA289
AGLY290
ALYS294
AHOH604
AHOH606

site_idAC4
Number of Residues5
Detailsbinding site for residue SO4 A 504
ChainResidue
AGLU79
ASER157
ATHR158
AGD501
AGD502

Functional Information from PROSITE/UniProt
site_idPS00629
Number of Residues13
DetailsIMP_1 Inositol monophosphatase family signature 1. W.VDPIDSTyqYiK
ChainResidueDetails
ATRP151-LYS163

site_idPS00630
Number of Residues15
DetailsIMP_2 Inositol monophosphatase family signature 2. WDsCAAhAILramGG
ChainResidueDetails
ATRP316-GLY330

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:33172890
ChainResidueDetails
AGLU80
AASP54

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:7947723, ECO:0000312|PDB:1INP
ChainResidueDetails
AASP153
AILE155
AASP317
AGLU79

site_idSWS_FT_FI3
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:33172890, ECO:0007744|PDB:7KIR
ChainResidueDetails
ATHR158
ASER268
ALYS270
AGLY290
AALA291
ALYS294
ATHR312
ASER157
AASP156

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P49441
ChainResidueDetails
ASER318

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 856
ChainResidueDetails
AASP54electrostatic stabiliser, proton acceptor, proton donor
AGLU79metal ligand
AASP153metal ligand
AILE155metal ligand
AASP156metal ligand
ATHR158electrostatic stabiliser, enhance reactivity, increase nucleophilicity, proton acceptor, proton donor, proton relay
AASP317metal ligand

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon