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1ZZW

Crystal Structure of catalytic domain of Human MAP Kinase Phosphatase 5

Functional Information from GO Data
ChainGOidnamespacecontents
A0006470biological_processprotein dephosphorylation
A0016311biological_processdephosphorylation
A0017017molecular_functionMAP kinase tyrosine/serine/threonine phosphatase activity
B0006470biological_processprotein dephosphorylation
B0016311biological_processdephosphorylation
B0017017molecular_functionMAP kinase tyrosine/serine/threonine phosphatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
AASP377
ACYS408
AGLN409
AALA410
AGLY411
AVAL412
ASER413
AARG414

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 502
ChainResidue
BCYS408
BGLN409
BALA410
BGLY411
BVAL412
BSER413
BARG414
BHOH226

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 503
ChainResidue
BHOH255
BSER413
BTHR417
BILE445
BSER446
BASN448
BPHE451

Functional Information from PROSITE/UniProt
site_idPS00383
Number of Residues11
DetailsTYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. IHCqaGvsRSA
ChainResidueDetails
AILE406-ALA416

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues286
DetailsDomain: {"description":"Tyrosine-protein phosphatase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00160","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Phosphocysteine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00160","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16806267","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17400920","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

251174

PDB entries from 2026-03-25

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