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5QU2

Crystal Structure of human Nck SH3.1 in complex with peptide PPPVPNPDY

Functional Information from GO Data
ChainGOidnamespacecontents
A0003779molecular_functionactin binding
A0035591molecular_functionsignaling adaptor activity
A0051016biological_processbarbed-end actin filament capping
A0051017biological_processactin filament bundle assembly
B0003779molecular_functionactin binding
B0035591molecular_functionsignaling adaptor activity
B0051016biological_processbarbed-end actin filament capping
B0051017biological_processactin filament bundle assembly
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue SO4 A 101
ChainResidue
AARG56
AHOH227
AHOH247

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 A 102
ChainResidue
AARG26
AASN44
AHOH202

site_idAC3
Number of Residues8
Detailsbinding site for residue SO4 D 201
ChainResidue
DPRO184
DASN185
DHOH301
DHOH303
DHOH309
AHOH210
BGLN14
BHOH130

site_idAC4
Number of Residues2
Detailsbinding site for Di-peptide ACE D 179 and PRO D 180
ChainResidue
APHE9
DPRO181

site_idAC5
Number of Residues3
Detailsbinding site for Di-peptide ACE E 179 and PRO E 180
ChainResidue
BPHE9
BTYR53
EPRO181

site_idAC6
Number of Residues10
Detailsbinding site for Di-peptide TYR E 188 and NH2 E 189
ChainResidue
BGLN15
BGLU18
BLYS34
BPHE48
BHOH115
EPRO186
EPRO186
EASP187
EASP187
EHOH302

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000255|PROSITE-ProRule:PRU00379, ECO:0000269|PubMed:9698567, ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:19690332
ChainResidueDetails
DTYR188
ETYR188

224572

PDB entries from 2024-09-04

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