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6PCK

Crystal structure of human diphosphoinositol polyphosphate phosphohydrolase 1 in complex with 1-IP7

Functional Information from GO Data
ChainGOidnamespacecontents
A0016462molecular_functionpyrophosphatase activity
A0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues32
Detailsbinding site for residue O81 A 201
ChainResidue
AARG10
AGLY52
AGLU66
AGLU70
AARG89
AHIS91
AARG115
ALYS133
AMG202
AHOH309
AHOH313
ALYS18
AHOH314
AHOH315
AHOH318
AHOH339
AHOH350
AHOH353
AHOH354
AHOH364
AHOH367
AHOH380
AARG20
AHOH384
AHOH396
AHOH444
ASER39
ASER40
AARG41
AILE47
AGLY50
AGLY51

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 202
ChainResidue
AGLY50
AGLY51
AGLU70
AO81201
AHOH313

site_idAC3
Number of Residues3
Detailsbinding site for residue CL A 203
ChainResidue
AASN86
AHIS91
AGLN136

site_idAC4
Number of Residues7
Detailsbinding site for residue CL A 204
ChainResidue
AARG27
ASER28
ASER30
AGLU31
AGLU32
AGLU33
AHOH480

Functional Information from PROSITE/UniProt
site_idPS00893
Number of Residues22
DetailsNUDIX_BOX Nudix box signature. GgmepeEepsvAAvREVcEEaG
ChainResidueDetails
AGLY51-GLY72

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305
ChainResidueDetails
AGLU69

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:19585659, ECO:0007744|PDB:2FVV, ECO:0007744|PDB:2Q9P
ChainResidueDetails
AARG10
ALYS18
ASER39
AARG89
ALYS133

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:19585659, ECO:0007744|PDB:2Q9P
ChainResidueDetails
AGLY50
AGLU66
AGLU70
AARG115

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22814378
ChainResidueDetails
AMET1

222624

PDB entries from 2024-07-17

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