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6AK7

Crystal structure of PPM1K-N94K

Functional Information from GO Data
ChainGOidnamespacecontents
A0004722molecular_functionprotein serine/threonine phosphatase activity
A0006470biological_processprotein dephosphorylation
A0043169molecular_functioncation binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue BME A 501
ChainResidue
AVAL95
ACYS97
AASN320
AHIS324

site_idAC2
Number of Residues3
Detailsbinding site for residue BME A 502
ChainResidue
ACYS145
AASP148
AGLU166

site_idAC3
Number of Residues1
Detailsbinding site for residue BME A 503
ChainResidue
ACYS316

site_idAC4
Number of Residues7
Detailsbinding site for residue MG A 504
ChainResidue
AASP298
AASP337
AMG505
AHOH619
AHOH627
AHOH646
AASP127

site_idAC5
Number of Residues7
Detailsbinding site for residue MG A 505
ChainResidue
AASP127
AGLY128
AMG504
AHOH601
AHOH604
AHOH622
AHOH646

site_idAC6
Number of Residues6
Detailsbinding site for residue MG A 506
ChainResidue
AASP112
AGLU143
AHOH608
AHOH614
AHOH618
AHOH637

site_idAC7
Number of Residues6
Detailsbinding site for residue MG A 507
ChainResidue
AASP208
AASP298
AHOH619
AHOH626
AHOH634
AHOH701

Functional Information from PROSITE/UniProt
site_idPS01032
Number of Residues9
DetailsPPM_1 PPM-type phosphatase domain signature. YFAVYDGHG
ChainResidueDetails
ATYR122-GLY130

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22291014","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4DA1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22291014","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2IQ1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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